See discussions, stats, and author profiles for this publication at: https://www.researchgate.

net/publication/324106484

Applied and Emerging Methods for Meat Tenderization: A Comparative

Perspective

Article  in  Comprehensive Reviews in Food Science and Food Safety · March 2018

DOI: 10.1111/1541-4337.12356

CITATIONS READS

15 837

4 authors, including:

Zuhaib Bhat Sue Mason

Lincoln University New Zealand Lincoln University New Zealand
83 PUBLICATIONS   1,030 CITATIONS    51 PUBLICATIONS   638 CITATIONS   

SEE PROFILE SEE PROFILE

Alaa El-Din Bekhit

University of Otago
275 PUBLICATIONS   3,677 CITATIONS   

SEE PROFILE

Some of the authors of this publication are also working on these related projects:

Boosting exports of the emerging New Zealand Dairy Sheep industry View project

Smart Utilization of Bioresources View project

All content following this page was uploaded by Zuhaib Bhat on 20 September 2018.

The user has requested enhancement of the downloaded file.

Applied and Emerging Methods for Meat
Tenderization: A Comparative Perspective
Zuhaib F. Bhat , James D. Morton , Susan L. Mason , and Alaa El-Din A. Bekhit

Abstract: The tenderization process, which can be influenced by both pre- and post-slaughter interventions, begins
immediately after an animal’s death and is followed with the disruption of the muscle structure by endogenous proteolytic
systems. The post-slaughter technological interventions like electrical stimulation, suspension methods, blade tenderiza-
tion, tumbling, use of exogenous enzymes, and traditional aging are some of the methods currently employed by the
meat industry for improving tenderness. Over the time, technological advancement resulted in development of several
novel methods, for maximizing the tenderness, which are being projected as quick, economical, nonthermal, green, and
energy-efficient technologies. Comparison of these advanced technological methods with the current applied industrial
methods is necessary to understand the feasibility and benefits of the novel technology. This review discusses the benefits
and advantages of different emerging tenderization techniques such as hydrodynamic-pressure processing, high-pressure
processing, pulsed electric field, ultrasound, SmartStretch , Pi-Vac Elasto-Pack
TM
R
system, and some of the current applied
methods used in the meat industry.
Keywords: conventional methods, high-pressure processing hydrodynamic-pressure processing, meat tenderization, pulsed
electric field, ultrasound

Introduction qualities represents a major cause of consumer dissatisfaction with

The demand for high-quality meat, and in particular red meat,
is expected to increase (Mullena et al., 2017) with eating quality
being the most important factor in the consumers’ choice of meat
(Thorslund, Sandøe, Aaslyng, & Lassen, 2016). Flavor, juiciness,
and tenderness are the three main attributes which influence the
sensory enjoyment of meat (Aaslyng & Meinert, 2017; Grunert,
Bredahl, & Brunsø, 2004; Picard and Gagaoua 2017). Defined as
“the ease, perceived by the consumer, with which meat struc-
ture is disorganized during mastication (Lepetit & Culioli, 1992),
tenderness has been shown to have the largest role in consumer
purchasing decisions (Mennecke, Townsend, Hayes, & Lonergan,
2007; Morton, Bhat, & Bekhit, 2018; Mullena et al., 2017; Wang,
Han, Ma, Yu, & Zhao, 2017a; Wu, Fu, Therkildsen, Li X, &
Dai, 2015) and in particular repeat buying (Miller, Carr, Ramsey,
Crockett, & Hoover, 2001).” It is also the most variable of all
meat palatability traits and is influenced by a range of biological
and environmental factors. The high level of variation in sensory
CRF3-2017-0248 Submitted 12/14/2017, Accepted 3/27/2018. Author Bhat
is with Dept. of Wine Food and Molecular Biosciences, Faculty of Agriculture and
Life Sciences, Lincoln Univ., Lincoln 7647, Christchurch, New Zealand. Author
Morton is with Dept. of Wine Food and Molecular Biosciences, Faculty of Agricul-
ture and Life Sciences, Lincoln Univ., Lincoln 7647, Christchurch, New Zealand.
Author Mason is with Dept. of Wine Food and Molecular Biosciences, Faculty of
Agriculture and Life Sciences, Lincoln Univ., Lincoln 7647, Christchurch, New
Zealand. Author Bekhit is with Dept. of Food Sciences, Univ. of Otago, P.O.
Box 56, Dunedin 9054, New Zealand. Direct inquiries to author Morton (E-mail:
James.Morton@lincolnuni.ac.nz)
beef (Ellies-Oury et al., 2016) with variability of tenderness as the
largest concern (Picard & Gagaoua, 2017).
The tenderness of a piece of meat is a result of several
factors which can be considered sequentially. The “background
toughness” is determined by the characteristics of the muscle
particularly its connective tissue (collagen), both its amount and
type (Veiseth, Shackelford, Wheeler, & Koohmaraie, 2004). This,
in turn, depends on factors like species, animal age, state of nutri-
tion, sex, and muscle type (Klont, Brocks, & Eikelenboom, 1998;
Wheeler, Shackelford, & Koohmaraie, 2000). Different muscle
fiber-types vary in their content of collagen and thus muscles
with different fiber-type composition also vary in their tenderness
(Maltin, Balcerzak, Tilley, & Delday, 2003; Marino, della Malva,
& Albenzio, 2015). Slow-twitch muscles contain more collagen
and have been reported as less tender (Kovanen, Suominen, &
Heikkinen, 1984). There is also a correlation with fiber diameter
and muscles with small fibers have been reported as more tender in
cattle and in pigs (Karlsson et al., 1993; Renand, Picard, Touraille,
Berge, & Lepetit, 2001). There is also evidence of correlations
with the overall amount of lipid, the level of intramuscular fat
(Lonergan et al., 2007; Smith et al., 2008) and the intra-fiber water
content (Offer et al., 1989). This muscle composition is fixed at
slaughter.
The two key factors after slaughter which determine the final
tenderness are the sarcomere length when the muscle goes into
rigor (Rhee, Wheeler, Shackelford, & Koohmaraie, 2004) and,
the duration and extent of any aging (Koohmaraie & Geesink,
2006). These are influenced by the state of the animal at slaughter


C 2018 Institute of Food Technologists®

doi: 10.1111/1541-4337.12356 Vol. 0, 2018 r Comprehensive Reviews in Food Science and Food Safety 1
Advanced methods for meat tenderization . . .

Table 1–Comparison of some novel meat tenderization technologies with some applied industrial techniques.

Handling
and
Level of potential
technical Energy cross con- Adoption by Tenderizing
Technologies Cost inputs consumption Process time tamination industry effect
Emerging tenderization methods
Hydrodynamic-pressure ↑ ↑ ↓ ↓ ↓ ↓ ↑
processing
High-pressure processing ↑ ↑ ↑ ↓ ↓ ↓ ↑
Ultrasound ↑ ↑ ↑ ↓ ↓ ↓ ↑
Pulsed electric field ↑ ↑ ↓ ↓ ↓ ↓ ↑
TM
SmartStretch / ↓ ↑ ↓ ↑ ↓ ↓ ↓
TM
Smartshape
Tenderbound ↓ ↑ ↓ ↑ ↓ ↑ ↑
Applied industrial methods
Tenderstretch ↓ ↓ ↓ ↑ ↓ ↓ ↓
Tendercut ↓ ↓ ↓ ↑ ↓ ↓ ↓
Blade (needle) ↓ ↓ ↓ ↓ ↑ ↑ ↑
tenderization
Tumbling ↓ ↓ ↑ ↑ ↑ ↑ ↑
Marination/Infusion/ ↓ ↓ ↓ ↑ ↑ ↑ ↑
Injection
Electrical stimulation ↓ ↓ ↓ ↓ ↓ ↑ ↑
Exogenous enzymes ↓ ↑ ↓ ↑ ↑ ↓ ↑
Aging ↓ ↓ ↑ ↑ ↓ ↑ ↑

as a result of management factors like age, diet, finishing regime, aging although other proteases are also involved (Geesink, Kuchay,
stress, and preslaughter handling (Andersen, Oksbjerg, Young, & Chishti, & Koohmaraie, 2006; Morton, Bickerstaffe, Kent, Drans-
Therkildsen, 2005; Ferguson & Warner, 2008; Geesink, Mareko, field, & Keeley, 1999).
Morton, & Bickerstaffe, 2001) and also postslaughter changes such Aging can also add some undesirable characteristics (Khan, Jung,
as the rate of pH decline (Melody et al., 2004), the ultimate pH Nam, & Jo, 2016). Drip loss increases with longer aging times and
(Lonergan et al., 2007) and the endpoint temperature (Obuz, higher temperatures, but cooking losses tend to decrease with
Dikeman, & Loughin, 2003). Variation in tenderness still exist, increasing aging time. Intermediate aging periods (4 to 7 days)
even if all of these attributes are controlled across muscles and may cause more cooking losses (Bekhit, Carne, Ha, & Franks,
it has proven a very elusive trait to predict and manage. It is 2014d). Although aging is a common method of tenderization
not an exaggeration to affirm that meat produced by each ani- and is very effective in improving the palatability of meat cuts that
mal is a “unique meat” with its own evolution (Lana & Zolla, have relatively small amounts of connective tissue and have not
2016). been cold-shortened, it has economic considerations in terms of
The meat industry needs to deliver consistent, high-quality meat space, time, labor, and energy.
in order to satisfy consumers, and increase consumption frequency
(Channon, D’Souza, & Dunshe, 2016). The industry has de- Electrical interventions
veloped a number of techniques (Hutchison, Mulley, Wiklund, The contraction of muscle in living animals is a result of an
Flesch, & Sims, 2014) to achieve this ranging from traditional electrical signal from the nerves leading to the release of calcium
aging to novel methods such as hydrodynamic-pressure process- within the muscle cells. Application of electric current or electric
ing. These can be broadly classified, based on their mechanism field can also cause contraction in postmortem muscle and lead
of action, into electrical, mechanical, chemical, and enzymatic to both biochemical and physical changes in the meat. Electrical
interventions. Table 1 compares some novel meat tenderization interventions can be used at several stages during processing in-
technologies with applied industrial techniques. cluding electrical stunning and the use of electricity to prevent
twitching during carcass dressing, which could endanger the meat
Traditional aging workers. However, the focus in this review will be on the two pro-
It has long been known that holding carcasses for days or weeks cesses which are known to affect tenderness, electrical stimulation,
after slaughter improves both the texture and the flavor of meat and pulsed electric field (PEF).
(Sitz, Calkins, Feuz, Umberger, & Eskridge, 2006; Piao et al.,
2015). Also known as “ripening” or “conditioning,” aging in- Electrical stimulation
volves holding carcasses, primals, or subprimals for a specific pe- The development of electrical stimulation dates back to the
riod under controlled refrigerated conditions to avoid microbial 1950s (Troy & Kerry, 2010) and it was commercially introduced
spoilage. Besides improved tenderness, mouthfeel, and juiciness in New Zealand in the 1970s to manage toughening due to cold-
(Irurueta, Cadoppi, Langman, Grigioni, & Carduza, 2008), aged shortening by the rapid freezing of lamb carcasses (Strydom &
beef possesses a peculiar salty or roasted or buttery flavor in com- Frylinck, 2014). Electrical stimulation is now widely used in many
parison to unaged beef (Gorraiz, Beriain, Chasco, & Insausti, 2002; meat-producing countries including New Zealand, Australia, the
Bruce, Beilken, & Leppard, 2005). Several biochemical processes USA, South Africa, India, and some European countries. Elec-
including lipolysis and oxidation are involved during postmortem trical stimulation leads to accelerated postmortem glycolysis with
aging of meat but the most important process for tenderness is the production of lactic acid, which ensures that the pH of the
proteolysis of the myofibrils. There is strong evidence supporting meat falls to below 6.0 before the muscle temperature reaches
the central role of the calcium-dependent protease, calpain 1, in 10 °C. This reduces the risk of cold shortening during rapid

2 Comprehensive Reviews in Food Science and Food Safety r Vol. 0, 2018 

C 2018 Institute of Food Technologists®
Advanced methods for meat tenderization . . .

Table 2–Findings of various studies elucidating the effect of pulsed electric field on the tenderness of different muscles.

Authors Muscle studied Muscle status PEF treatment Findings

Khan et al. (2017) Longissimus et lumborum Post-rigor 2.5 kV, 200 Hz, 20 μs; 10 kV, 200 Hz, 20 Tenderness was not affected
(beef) μs (0.23 to 0.68 kV/cm) by pulsed electric field.
Faridnia, Bremer, Biceps femoris (beef) Post-rigor 1.7 kV/cm, 50 Hz, 20 μs Significant reduction in shear
Burritt, and Oey force.
(2016)
Suwandy et al. Longissimus lumborum Pre-rigor 5 kV, 10 kV × 20, 50, 90 Hz Tenderness decreased with
(2015b) and semimembranosus treatment intensity in
(beef) longissimus lumborum and
increased regardless of
intensity in
semimembranosus.
Bekhit et al. Longissimus lumborum Post-rigor 5 kV, 10 kV × 20, 50, 90 Hz (0.27 to Tenderness increased
(2014c) and semimembranosus 0.56 kV/cm) regardless of intensity in
(beef) longissimus lumborum and
with intensity in
semimembranosus.
Bekhit et al. Longissimus lumborum Pre-rigor Repeated (1 ×, 2 ×, 3 ×) PEF treatment 1× and 2× treatment had no
(2016) and semimembranosus (10 kV, 90 Hz, 20 μs) effect whereas 3× PEF
(beef) treatment reduced
tenderness in longissimus
lumborum, tenderness
increased with lowest shear
force in 3× PEF treatment
in Semimembranosus.
Suwandy et al. Longissimus lumborum Post-rigor Repeated (1 ×, 2 ×, 3 ×) PEF treatment Tenderness increased with
(2015d) and semimembranosus (10 kV, 90 Hz, 20 μs) repeated treatments in
(beef) longissimus lumborum and
had no effect on
semimembranosus.
Suwandy et al. Longissimus lumborum Post-rigor 5 kV, 10 kV × 20, 50, 90 Hz Tenderness increased
(2015a) and semimembranosus regardless of intensity in
(beef) longissimus lumborum and
with treatment intensity in
semimembranosus.
Faridnia, Bekhit, Longissimus thoracis Post-rigor 0.2 to 0.6 kV/cm, 1 to 50 Hz, 20 μs Tenderness of the samples
Niven, and Oey (beef) was not affected by PEF.
(2014)
Faridnia et al. Semitendinosus (beef) Post-rigor 1.4 kV/cm, 50 Hz, 20 μs Tenderness was not affected
(2015) by PEF alone. In
combination with
freezing-thawing, PEF
improved tenderness.
McDonnell et al. Longissimus thoracis et Post-rigor 1.2 or 2.3 kV/cm x 100 or 200 Hz x 150 No effect was observed on
(2014) lumborum (pork) or 300 pulses texture of the samples.
Arroyo et al. Breast meat (turkey) Post-rigor 7.5, 10, 12.5 kV (fresh meat), 14, 20, 25 No effect was observed on
(2015a) kV (frozen meat) x 10, 55, 110 Hz (up tenderness of the samples.
to 3 kV/cm)
Arroyo et al. Longissimus thoracis et Post-rigor 1.4 kV/cm, 10 Hz, 20 μs, 300 and 600 No effect was observed on
(2015b) lumborum (beef) pulses shear force, although
samples showed tendency
towards reducing
toughness.
O’Dowd et al. Semitendinosus (beef) Post-rigor 1.9 kV/cm, 65 Hz, 20 μs Tenderness was not affected
(2013) by PEF.
Toepfl (2006) Pork shoulder, beef meat Post-rigor 0.5 to 5 kV/cm, 50 to 1,000 pulses, 1 to Tenderness increased in
25 kJ/kg treated samples.

chilling of carcasses, but electrical stimulation also accelerates meat
tenderization by increasing the rate of proteolysis and by physi-
cally disrupting the muscle fibers (Hwang, Devine, & Hopkins,
2003; Lang et al., 2016). It may also improve the tenderness of
meat by disrupting the membranes of lysosomes and releasing the
cathepsins at low pH and high temperature (Dutson, Smith, &
Carpenter, 1980). The physical disruption of muscle fibers by se-
vere contractions and reduction in cross-linking of the collagen
molecules may also contribute to tenderness (Judge, Reeves, &
Aberle, 1980).
The impact of electrical stimulation on pH drop and meat qual-
ity depends on several factors, such as voltage, frequency, dura-
tion, and the method of application (Polidori, Ariani, Micozzi,
& Vincenzetti, 2016) and, accordingly, several forms of electrical
stimulation devices are available which differ in voltage, current,
frequency of pulses, and waveforms (Simmons et al., 2008). The
meat industry often demarcates the range of application of voltage
into two types, high voltage (300 to 1,000 V) and low (50 to 120
V) voltage (Troy & Kerry, 2010). High-voltage stimulation pro-
duces a greater rate of pH decline, which is more consistent and
less variable (Simmons et al., 2008), but it is more expensive and
requires greater safety precautions. Although high-voltage elec-
trical stimulation delivers favorable results in all circumstances,
low-voltage systems have been reported to be equally effective as
long as the duration of stimulation is not too short, that is >40 s as
opposed to 10 s (Gursansky, O’Halloran, Egan, & Devine, 2010).
Several studies have demonstrated equal efficacy of low-voltage
stimulation on pH drop and improvement in tenderness (Eikelem-
boom, Smulders, & Ruderus, 1985; Hwang & Thompson, 2001;
Polidori, Lee, Kauffman, & Marsh, 1999). Safety concerns about
high voltage are also a factor in commercial plants (Hopkins,
Toohey, Pearce, & Richards, 2008).


C 2018 Institute of Food Technologists® Vol. 0, 2018 r Comprehensive Reviews in Food Science and Food Safety 3
Advanced methods for meat tenderization . . .

Table 3–Findings of various studies elucidating the effect of hydrodynamic-pressure processing on the tenderness of different muscles.

Authors Muscle studied Treatment Findings

Bolumar et al. (2014)
Zuckerman et al.
(2013)
Schilling et al. (2002)
Bowker et al. (2008)
Moeller et al. (1999)
Solomon, Carpenter,
Snowder, & Cockett
(1998)
Bowker et al. (2010)
Meek et al. (2000)
Claus et al. (2001)
Solomon, Long, and
Eastridge (1997)
Beef loin steaks One single pulse, 36 kV (11,664 J per
pulse), 20 cm distance from meat
to spark (prototype based on
electrical discharge under water).
Beef semimembranosus 150 g of explosives were detonated
35.6 cm above the surface of the
meat (plastic container), 450 g of
explosives were detonated 61.0 cm
above the surface of the meat
(stainless steel commercial
prototype unit).
Beef biceps femoris 105, 200, and 305 g of explosives
were detonated 26.7 cm far from
the meat, 83, 104, 124 MPa
pressure.
Beef strip loin 100 g of explosives were detonated
31 cm far from the meat.
Pork loin 150 g of explosives were detonated
36 cm far from the meat, 68.9 MPa
pressure.
Lamb longissimus 100 g of explosives were detonated
30.5 cm far from the meat, 60 to
70 MPa pressure.
Turkey breast 100 g of explosives were detonated
31.0 cm far from the meat, 98 L
container, 40 cm diameter, 1.3 cm
thick steel plate.
Chicken breast 200, 275, 350, and 350 g of
explosives were detonated 20.0,
20.0, 20.0, and 23.0 cm,
respectively.
Chicken breast 40 g of explosives were detonated,
stainless steel research prototype.
Beef longissimus 50, 75, 100 g of explosives were
detonated 30.5 cm far from the
meat, 60 to 70 MPa pressure.
18% reduction in
Warner-Bratzler shear
force.
37% reduction in
Warner-Bratzler shear force
in plastic container and
25% in steel commercial
unit immediately
post-treatment.
Disrupted the integrity of the
collagen fibril network of
the endomysium.
Tenderness improved with
reduction in shear force by
up to 24%.
Tenderness improved with
reduction in shear force by
up to 23%.
Tenderness improved with
reduction in shear force by
up to 17%.
Tenderness improved with
reduction in shear force by
up to 67%.
Up to 13% reduction in shear
force
Up to 28% reduction in shear
force
Up to 42% reduction in shear
force
Tenderness improved with
reduction in shear force by
up to 68%.

Although application of electrical stimulation can have a tender-
ization gain, its effect on pH decline during early postmortem can
have a great impact on other proteins and enzymatic systems that
control meat quality characteristics such as water-holding capacity,
meat color, and stability. Negative effects of electrical stimulation
on color stability and water holding capacity have been reported in
some cases (Adeyemi & Sazili, 2014; Bekhit et al., 2014d). How-
ever, application of electrical stimulation has also been reported to
improve color in beef (McKenna, Maddock, & Savell, 2003), pork
(Taylor & Martoccia, 1995), venison (Wiklund, Stevenson-Barry,
Duncan, & Littlejohn, 2001), lamb (Polidori et al., 1999), chevon
(Cetin & Topcu, 2009), and chicken (Young, Buhr, & Lyon, 1999).
Bekhit et al. (2014d) reported increased drip loss due to protein
denaturation when the chilling rate was low, as in large carcasses
or those with a thick fat layer, although other workers have re-
ported no adverse effect of electrical stimulation on meat color
stability, water-holding capacity, and drip loss (Li, Li, Li, Hviid, &
Lundström, 2011; Sánchez, Pérez, Barreras, Figueroa, & Herrera,
2016; Wiklund et al., 2001).
Pulsed electric field
PEF is a novel technology that was first applied commercially
to sterilize fruit juice (Clark, 2006). During PEF processing,
food is passed through or placed between two electrodes and
exposed to electric field pulses of short duration in the range
of several nanoseconds to several milliseconds with an electric
field strength of 0.1 to 80 kV/cm (Barba and others 2018; Bhat,
Morton, Mason, & Bekhit, 2018; Puértolas & Barba, 2016). The
shorter processing time and lower treatment temperatures of PEF
compared to traditional processing technologies and the poten-
tial for continuous flow (Puertolas, Saldana, Condon, Alvarez, &
Raso, 2010; Walkling-Ribeiro, Rodrı́guez-Gonzalez, Jayaram, &
Griffiths, 2011) make it a very appealing technology for food pro-
cessors (Bhat et al., 2018). PEF has attracted the attention of meat
scientists due to its ability to alter membrane properties (Barba,
Grimi, & Vorobiev, 2014; Bhat et al., 2018; Deng et al., 2014)
and potentially affect the activity of calpains and thus influence
the rate and extent of tenderization during aging. It is also able
to modify several quality characteristics of meat (such as color,
texture, and water-holding capacity) and enhance mass transfer
processes (such as brining and curing) due to its potential for
cell membrane permeabilization (Gudmundsson & Hafsteinsson,
2001; O’Dowd, Arimi, Noci, Cronin, & Lyng, 2013; McDonnell,
Allen, Chardonnereau, Arimi, & Lyng, 2014). As the wider use
of PEF in meat has been reviewed recently (Bhat et al., 2018) this
paper will focus on tenderness.
Several studies have confirmed the potential of PEF for improv-
ing the tenderness of muscles during aging (Bekhit, Suwandy,
Carne, van de Ven, & Hopkins, 2016; Faridnia et al., 2015;
Khan et al., 2017; Ma et al., 2016; Suwandy, Carne, van de
Ven, Bekhit, & Hopkins, 2015a, 2015b, 2015c, 2015d). Un-
like other methods, such as electrical stimulation or Tenderstretch
TM, which do not affect all muscles equally, PEF is a stand-alone
technology where process parameters can be optimized for dif-
ferent muscles (Suwandy et al., 2015a). It also has limited side
effects, such as severe structural and oxidative changes and off-
flavor development, in comparison with some other methods
of tenderization (Bekhit, Carne, Ha, & Franks, 2014a; Bekhit,

4 Comprehensive Reviews in Food Science and Food Safety r Vol. 0, 2018 

C 2018 Institute of Food Technologists®
Advanced methods for meat tenderization . . .

Table 4–Findings of various studies elucidating the effect of high-pressure processing on the tenderness of different muscles.

Authors Muscle studied Treatment Findings

Shao et al. (2018)
Morton et al. (2017)
Ros-Polski et al.
(2015)
Neto et al. (2015)
Sikes and Tume
(2014)
Grossi, Bolumar,
Søltoft-Jensen, and
Orlien (2014)
Mcardle et al. (2013)
Souza et al. (2012)
Duranton, Simonin,
Chéret, Guillou, and
De Lamballerie
(2012)
Canto et al. (2012)
Kruk et al. (2011)
Smit, Summerfield,
and Cannon (2010)
Schenkova et al.
(2007)
Kim, Lee, Lee, Kim, and
Yamamoto (2007b)
Ichinoseki, Nishiumi,
and Suzuki (2006)
Elgasim and Kennick
(1982)
Red swamp crayfish 0, 100, 200, 300, 400, and
(Procambarus clarkia) 500 MPa for 5 min (25 to
28 °C)
Beef longissimus thoracis 175 MPa for 3 min
250 MPa for 2 min
White ground chicken 50, 100, 200, or 300 MPa for
meat. 60, 120, or
180 s (ambient
temperature)
Beef longissimus dorsi 100, 200, 300, and 400 MPa,
15 min (5 to 18 °C)
Beef semimembranosus HPP-Heat: 200 MPa, 20 min
and biceps femoris. at 60, 64, 68, 72, or 76 °C
HPP-Heat and cook: 200
MPa, 20 min at 60 °C,
cooked at 80 °C for 30 min
Pork semitendinosus 600 MPa for 6 min (5 °C)
Lamb pectoralis profundus 200, 400, and 600 MPa for
20 min (20, 40, and 60 °C)
Pork longissimus dorsi 215 MPa for 15 s (29.4 °C)
Pork biceps femoris 500 MPa for 6 min (20 °C)
Alligator tail 200, 300, and 400 MPa for
10 min (20 °C)
Chicken breast 300, 450, and 600 MPa for
5 min (15 °C)
Pork longissimus dorsi 175 to 225 MPa for 5 to
180 s (<10 °C)
Beef longissimus 100, 200, and 300 MPa for
lumborum et thoracis 10 min (4 °C)
Beef semitendinosus 100 to 500 MPa for 5 min
(15 °C)
Beef shoulder 100 to 500 MPa for 5 min
(8 °C)
Beef longissimus dorsi 103 MPa for 2 min (37 °C)
Hardness of the samples
increased with increasing
pressure.
Tenderness increased in treated
samples (60% lower shear
force than chill aged meat after
1 day).
In general hardness of samples
increased treated at 200 and
300 MPa for 180 sec.
Tenderness improved (up to
21.12%) in samples treated at
100 or 200 MPa
Meat tenderness was improved at
temperatures above 64 °C and
was optimal at 76 °C.
Lower sensory scores were
obtained for tenderness
Lower shear force values were
observed for samples treated at
200 MPa at 60 °C (25.78 N) in
comparison to non-treated
control (37.63 N).
Tenderness increased in treated
muscles
Tenderness decreased with
applied pressure.
Hardness decreased in samples
treated at 200 MPa.
Hardness of samples treated at
450 MPa (44.8 kg) and 600
MPa (50.7 kg) increased in
comparison to untreated
control (28.0 kg).
Tenderness increased in treated
samples.
Tenderness increased
significantly at 100 MPa.
Higher pressures caused paler
color.
Shear force and hardness of
samples treated at 300 MPa
decreased significantly.
Tenderness increased with lowest
shear force observed at 100
MPa.
Tenderness improved with shear
force reduction (65%).

Hopkins, Geesink, Bekhit, & Franks, 2014b). PEF could be used
to optimize the quality of the less tender meat cuts by optimizing
the technological inputs to different meat cuts either pre-rigor
and post-rigor (Bekhit et al., 2016). This technology could be of
particular importance in the case of hot-boned muscles, which are
generally less tender than cold-boned muscles (White, O’Sullivan,
Troy, & O’Neill, 2006; Troy & Kerry, 2010) and could be treated
separately with different process parameters to obtain optimal re-
sults (Bekhit et al., 2016).
The mechanism where PEF operates through calcium release
and calpain activation is supported by the finding that a post-
mortem aging period is essential for gaining the tenderization
benefit of PEF (Bekhit, van de Ven, Suwandy, Fahri, & Hopkins,
2014c; Bekhit et al., 2016; Suwandy et al., 2015a, 2015b, 2015c;
Warner et al., 2017). PEF has been shown to increase the
proteolysis of desmin and troponin-T in beef muscles during
aging (Bekhit et al., 2016; Suwandy et al., 2015a, 2015b, 2015c).
Several studies have suggested the contribution of other factors
like physical disruption of muscles, release of cathepsins from
lysosomes, and accelerated glycolysis due to calcium release in
pre-rigor muscles to the positive effect of PEF on tenderization
(Bhat et al., 2018; Warner et al., 2017).
The potential of PEF to improve meat tenderness in beef mus-
cles appears to depend on several factors, including electric field
strength, the muscles under study, post-mortem status, and the
presence of an aging period. Although it is independent of initial
muscle pH and muscle fiber direction (orientation in the field;
Suwandy, Carne, van de Ven, Bekhit, & Hopkins, 2015c), a min-
imum electric field intensity seems to be needed for PEF to in-
crease the tenderness of a muscle during a proper aging period.
However, PEF has also been reported to have negative effects on
tenderness. High-intensity PEF (10 kV, 90 Hz) increased the shear


C 2018 Institute of Food Technologists® Vol. 0, 2018 r Comprehensive Reviews in Food Science and Food Safety 5
Advanced methods for meat tenderization . . .

Table 5–Findings of various studies elucidating the effect of ultrasound on the tenderness of different muscles.

Authors Muscle studied Treatment parameters Findings

Zou et al. (2018) Goose breast muscle 20 kHz, 15.6 W/cm2 , 20 min Ultrasound at 800 W (20 kHz) for
20 min effectively improved meat
tenderness during 0 to 24 hr
storage time (4 °C)
Wang et al. (2018) Beef semitendinosus 20/kHz, 25 W/cm2 , 20 or Ultrasound decreased
40 min Warner-Bratzler shear force
significantly at 3 and 7 day of
post-mortem aging.
Barekat & Beef longissimus 20 kHz, 100 and 300 W, 10, Ultrasound significantly decreased
Soltanizadeh lumborum 20, and 30 min Warner-Bratzler shear force.
(2017)
Kang et al. (2017) Beef longissimus dorsi 20 kHz, 150 and 300 W, 30 Ultrasound increased tenderness by
and 120 min increasing MFI values and
proteolysis of desmin and
troponin-T.
Chen et al. (2015) Chicken muscle 40 kHz, 1500 W, 30 and Low-frequency and high-power
60 min ultrasound improved disruption of
myofibrillar structures and
increased proteolysis.
Sikes et al. (2014) Beef longissimus 600 kHz, 320 W and 760 W, No added benefit of ultrasound
lumborum 48 kPa and 65 kPa acoustic treatment above that of the
pressures, 10 min. normal ageing process.
Ozuna et al. (2013) Pork longissimus dorsi 40 kHz, 37.5 W/dm2 Ultrasound increased the hardness.
continuously during
brining.
Smith, Cannon, Beef semitendinosus 26 kHz, 1000 W, 2 to 4 min Treatment lowered the shear force
Novakofsky, values.
Mckeith, and
O’brien (1991)
Jayasooriya et al. Beef longissimus thoracis 24 kHz, 12 W/cm2 , 0 to Increased tenderness by reducing the
(2007) et lumborum and 240 sec shear force values.
semitendinosus
Chang et al. (2009) Beef semitendinosus 40 kHz, 1500 W, 25 o C Hardness decreased with 10 min
treatment,
Reduced muscle fiber diameter and
thermal stability of collagen.
Stadnik and Beef semitendinosus 45 kHz, 2 W/cm2 , 120 sec Significant reduction in shear force
Dolatowski (2011)
Stadnik, Dolatowski, Beef semitendinosus 45 kHz, 2 W/cm2 , 120 sec Acceleration of the ageing process.
and Baranowska
(2008)
Xiong, Zhang, Zhang, Breast muscles of culled 24 KHz, 12 W/cm2 , 4 min Significant reduction in shear force.
and Wu (2012) hen
Dickens, Lyon, and Broiler breast muscle 40 kHz, 2400 W, 15 min Significant reduction in shear force.
Wilson (1991)
Pohlman, Dikeman, Beef semitendinosus and 20 kHz, 22 W/cm2 , 0.5 or Reduced hardness regardless of
and Zayas (1997) biceps femoris 10 min sonication time.
Hu et al. (2014) Jumbo squid (Dosidicus 20 to 140 kHz, 45 to 360 W, Desirable flexibility and firmness was
gigas) meat 10 to 50 min obtained.

force and toughened hot-boned beef loins (longissimus et lumborum;
Suwandy, Carne, van de Ven, Bekhit, & Hopkins, 2015b). It was
suggested that this was due to Ohmic heating during the pro-
cess, causing denaturation of the proteins and enzymes involved
in the tenderization. Table 2 presents the findings of various stud-
ies elucidating the effect of PEF on the tenderness of different
muscles.
Several studies have found no effect of PEF on color, water-
holding capacity, and lipid oxidation (Arroyo et al., 2015a, 2015b;
McDonnell et al., 2014; Faridnia and others 2014; Suwandy et al.,
2015c), but it did cause an increase in purge loss (Bekhit et al.,
2014c, 2016; Faridnia and others 2016; Suwandy, Carne, van de
Ven, Bekhit, & Hopkins, 2015d) and cooking loss (Suwandy et al.,
2015d). High PEF at high intensity (10 kV, 200 Hz, 20 μs) did
affect L∗ and a∗ values in beef and also a reduction in some minerals
(Khan et al., 2017, 2018). PEF has been reported to increase the
concentration of Cr in beef (Khan et al., 2018). It has also been
reported to increase the concentration of Ni in chicken breast
due to the possible release from electrodes (Khan et al., 2018).
Loss or gain of minerals during PEF processing seems to have
no commercial significance and there is no scientific evidence
regarding the hazardous or toxic effects of the technology (Kumar,
Patel, & Kumar, 2015; Pal, 2017).
In comparison to the traditional thermal pasteurization, non-
thermal processing technologies, like HPP and PEF, have a
higher environmental impact in terms of reduced CO2 production
(Sampedro, McAloon, Yee, Fan, & Geveke, 2014). Cost involved
in changing the plant design and high initial capital investments are
viewed as limitations in the uptake of these technologies, although
continuous PEF systems are considered as efficient, high-speed and
low maintenance (Jeyamkondan, Jayas, & Holley, 1999, Bhat et al.,
2018). PEF appears to be an ineffective technology for microbial
decontamination of fresh meat, although it is a novel nonthermal
technology for production of consumable quality liquid foods un-
der high-speed continuous process without compromising their
nutritional and sensorial quality. Inactivation of microbes in meat
requires high-intensity PEF treatments that will have an adverse
impact on nutritional and sensorial quality of meat. Such intense
treatments could also affect the tenderization process during aging
due to denaturation of the endogenous proteolytic enzymes by

6 Comprehensive Reviews in Food Science and Food Safety r Vol. 0, 2018 

C 2018 Institute of Food Technologists®
Advanced methods for meat tenderization . . .

Table 6–Findings of various studies involving the use of exogenous enzymes on the tenderness of meat.

Authors Enzymes used Meat source Findings

Sun et al. (2018) A novel aspartic protease Pork muscles Shear force decreased when RmproA
(RmproA) from Rhizomucor (22.5 N) and papain (22.2 N) were
miehei expressed in Pichia injected at 0.5 mg/g pork muscles.
pastoris (0.25 and 0.5 At a relatively low concentration
mg/100 g muscle). (0.25 mg/100 g), RmproA-treated
sample showed lower shear force
(26.7 N) than papain (27.9 N).
Zhang et al. (2017) Actinidin from Chinese Pork and rabbit Shear force was reduced by more than
Kiwifruit cultivars at a ratio longissimus dorsi half using the purified actinidin at
of 1:10 (mL of sample a dosage of 0.5 mg/100 g muscle
volume: g of initial weight in pork and rabbit muscle.
of muscle).
Barekat and Papain (0.1% enzyme Beef longissimus Significant decrease in filtering
Soltanizadeh solution) lumborum residue, Warner-Bratzler shear
(2017) force and textural parameters
Abdel-Naeem and Ginger extract (7%), papain Camel meat burger Significant increase in collagen
Mohamed (2016) (0.01%), and mixture of patties solubility and sensory scores by
ginger (5%), and papain using ginger, papain and their
(0.005%) mixture, significant reduction in
the shear force.
Bekhit et al. (2012) Commercial papain, Beef connective tissue Actinidin protease was most effective
bromelain, actinidin, and and topside myofibril at hydrolyzing beef myofibril
zingibain protease extracts proteins, zingibain protease was
most effective at hydrolyzing
connective tissue proteins.
Zhao et al. (2012) Cold-adapted collagenolytic Myofibrillar proteins from MCP-01 showed a unique
protease MCP-01, papain, beef muscle and casein tenderization mechanism
and bromelain compared to papain and bromelain,
MCP-01 had a strong selectivity for
degrading collagen at 4 o C.
Ha et al. (2013) Kiwifruit and asparagus Beef connective tissue Kiwifruit extract was more effective
enzyme extracts and topside myofibril at hydrolyzing myofibrillar and
extracts collagen proteins, potential of a
synergistic effect of these
proteases in improving the
tenderness.
Naveena et al. (2004) Cucumis trigonus Roxb Buffalo meat Increased collagen, sarcoplasmic, and
(Kachri) and Zingiber myofibrillar protein solubility,
officinale roscoe (ginger reduction in shear force in all
rhizome) treated samples.
He et al. (2015) Ginger extract Duck breast Significant decrease in shear force,
significant increase in myofibrillar
fragmentation index.
Han et al. (2009) Pre-rigor infusion of kiwifruit Lamb carcasses Significant decrease in shear force.
juice (10% body weight)
Ramezani, Aminlari, Ficin protease Beef treated muscles in Solubility of meat proteins increased.
and Fallahi (2003) sausages
Aminlari et al. (2009) Actinidin protease Beef muscles Tenderization increased (10%
decrease in shear force) when
treated at 37 °C for 2 hr.
Ahmet (2014) Bromelain (1.5%, 3%, and Duck breasts Significant reduction in shear force in
4.5%) all treated samples.
Manohar, Gayathri, Bromelain (1%, 2%, 3%, and Red meat Improvement in tenderness.
and Vishnupriy 4%)
(2016)
Doneva et al. (2015) Bromelain and papain Turkey meat Concentration and time-dependent
solution: 50, 100, 200 hydrolysis of collagen structural
U/mL × 24, 48, 72 hr elements
Whetstone, Adhikari, Bromelain solution Beef steaks (strip, Improvement in tenderness.
and Chamber 20 mg/mL chuck-eye, top blade)
(2014)
Nadzirah, Zainal, Bromelain powder Beef round cuts Bromelain decreased hardness.
Noriham, and
Normah (2016)
Qihe et al. (2006) Elastase from Bacillus sp. Beef muscles (shoulder) Marination time of 4 hr was found
EL31410 sufficient for enzyme adsorption. A
marked decrease in hardness was
observed and elastase was
proposed as a promising substitute
for papain.

the heat produced during batch mode. The primary applications
of PEF technology in food preservation are mostly limited to pas-
teurization (Saldaña, Álvarez, Condón, & Raso, 2014) as PEF fails
to inactivate bacterial spores that prevent its use for food and wa-
ter sterilization (Pillet, Formosa-Dague, Baaziz, Dague, & Rols,
2016).
Mechanical interventions
It has long been known that meat can be tenderized by dis-
ruption of the muscle structure with mechanical force. Chopping
or mincing of the meat is the simplest example of mechanical
tenderization of meat, however, it is accompanied by a decline in
price. A number of other techniques have been developed which


C 2018 Institute of Food Technologists® Vol. 0, 2018 r Comprehensive Reviews in Food Science and Food Safety 7
Advanced methods for meat tenderization . . .
are effective depending on the type and rigor status of the muscle.
Some operate pre-rigor by restricting the ability of the muscles to
contract or by stretching these muscles. Others are more suited to
post-rigor manipulation and improving tenderness of low-value,
high collagen meat cuts.
Pre-rigor methods
Conventionally beef and lamb carcasses are hung by the hind
of the leg or Achilles tendon (Achilles tendon suspension) pulling
the hind leg backward, with a slightly curved vertebral column, in
a position different from the standing animal’s configuration. This
reduces the skeletal restraint and allows more rigor contraction for
most muscles of the hind limb and along the vertebral column
(Ahnstrom, Hunt, & Lundström, 2012). Developed more than
40 yr ago, tenderstretching is an alternative postmortem processing
technique in which carcasses are suspended from the pelvic or hip
bone (obturator foramen), preventing muscle rigor contraction.
Also known as pelvic suspension, hip suspension or aitch-bone
hanging, this type of suspension allows the hind quarter to be in
a walking-like position which increases the tension of the muscles
on the hind leg and along the vertebral column (Hopkins, 2014).
This prevents the muscles from contracting causing an increase
in the sarcomere length. There is a well-established linkage be-
tween sarcomere length and improved tenderness (Hegarty and
Allen 1975; Hopkins, 2004; Locker & Hagyard, 1963; Marsh &
Leet, 1966). This method has been shown to increase tender-
ness of muscles in beef (Ahnstrom et al., 2012; Liu et al., 2016),
lamb (Thompson et al., 2005), venison (Hutchison et al., 2014),
pork (Bertram & Aaslyng, 2007), and alpaca (Smith, Bush, van
de Ven, & Hopkins, 2017). It has been reported to reduce drip
and cooking losses in beef (Bekhit et al., 2014d). Tenderstretching
is comparatively easy to apply and requires no specialized equip-
ment, however, it has only been adopted by a few processors
(Smith et al., 2017) due to its limited impact on many muscles and
other factors like less flexible, higher space requirements, and labor
cost.
Another method for carcass-stretching is the tendercut process,
developed at Virginia Polytechnic Institute and State Univ. in
the USA (Wang, Claus, & Marriott, 1994), where the skeleton
and connective tissue are separated leaving only the muscle to
hold the weight of the carcass below the split. It involved cutting
bones and connective tissue in the mid-loin and round/sirloin
junction of carcass sides (Sorheim & Hildrum, 2002) and improved
the tenderness of longisimus lumborum and muscles of the hind
quarter through Achilles tendon suspension. This method is also
not widely used in the meat industry and its limited adoption can
be explained by its variable results, utility in limited muscles, and
higher space and labor costs.
Two novel approaches have been developed using packaging to
TM TM
improve tenderness. SmartStretch /Smartshape is designed to
reduce the contraction of hot-boned primals during rigor or by
stretching these muscles. The system has been adopted commer-
cially in Australia (Hopkins, 2014) and uses external air pressure
to stretch and reform hot-boned primals into a uniform size and
retain the stretch during rigor by using restraining packaging. The
system requires specialized equipment to wrap the hot-boned pre-
rigor muscles. It is very flexible as it can be applied to any target
muscles but behaves differently with meat from different species
and seems to be more effective in the case of sheep meat than
beef. Several studies (Taylor et al., 2010, 2011; Toohey, van de
Ven, Thompson, Geesink, & Hopkins, 2012c; Taylor, Toohey, van
TM
de Ven, & Hopkins, 2013) examined the effect of SmartStretch
8 Comprehensive Reviews in Food Science and Food Safety r Vol. 0, 2018
treatment on different beef muscles and reported no overall sig-
nificant change in measured shear force values of the muscles. In
contrast, significant improvements have been reported in the ten-
TM
derness of sheep muscles after SmartStretch treatment. Applying
TM
the SmartStretch treatment using a prototype stretching device
to hot-boned sheep topsides (semimembranosus) caused a significant
reduction in shear compared to nonstretched meat (Toohey, van
de Ven, Thompson, Geesink, & Hopkins, 2012a). Another study
TM
using SmartStretch on sheep muscles resulted in longer sar-
comeres for both the semimembranosus and semitendinosus muscles
(Toohey, van de Ven, Thompson, Geesink, & Hopkins, 2012b).
SmartstretchTM treatment has the potential to eliminate the need
of long-processing storage (aging) in pre-rigor sheep muscles to
achieve acceptable tenderness (Toohey, van de Ven, Thompson,
Geesink, & Hopkins, 2013). The Tenderbound or Pi-Vac Elasto-
R
Pack system, other packaging-based approach to tenderness, uses
highly elastic wrapping material, like elastic film tubes or sleeves,
which are stretched by using a vacuum to enable the introduction
of a piece of meat. Once the meat is inside the film sleeve, the vac-
uum is released, and the film retracts and prevent the contraction
of meat by hindering radial expansion during rigor development
by exerting longitudinal forces on the meat. This system has been
adopted commercially in Europe (Hopkins, 2014) and requires
specialized equipment. Besides improving tenderness and reduc-
ing drip loss, other advantages of the system are saving space (no
chilling room), energy (not having to chill whole carcass), and time
(muscles cool more rapidly), and it is environmentally friendly
by reducing the use of packaging materials (Taylor & Hopkins,
2011).
Post-rigor methods
The meat industry has also used mechanical techniques to ten-
derize the inherently tougher cuts of meat. Blade or needle tender-
ization is one of the most effective and efficient technologies used
to improve the tenderness of less tender cuts of meat (Pietrasik &
Shand, 2011). It involves the partial destruction of connective tis-
sue and severance of muscle fibers by using closely spaced needles
or thin blades having sharpened edges which physically disrupt
muscle fibers and connective tissues leading to reduced resistance
to shear force (Pietrasik & Shand, 2004). Blade tenderization is
used on raw product, generally after rigor (post-rigor) and the
primal and sub-primal cuts could be tenderized before or after
packaging and aging with equal effectiveness (Maddock, 2008).
Blade tenderization is usually done at the processing plant or meat
distributor level and is an accepted technology. It can, however,
result in potential microbial contamination in the penetration areas
due to the transfer of pathogens to the interior of meat and affect
the appearance and color of the steaks (Bolumar & Toepfl, 2016).
Depending on the muscle and meat cut, it can also affect the
flavor and significantly reduce the intensity of the flavor (Bekhit
et al., 2014d). The equipment used to tenderize large cuts is also
generally large and expensive.
Tumbling (massaging) of meat tissue is equally acceptable and is
recognized in the meat industry as blade tenderization. It involves
the disruption of the muscle structure to disintegrate external
surfaces of meat and release of myofibrillar proteins. During this
process the meat pieces are kneaded in rotating drums, allowing the
meat to gain energy by friction and free falling. It affects the meat
structure by cellular disruption which allows increased protein
extractability causing greater solubilization of muscle proteins. The
mechanical improvement in tenderness with tumbling is secondary
to moisture or flavor addition (Maddock, 2008).

C 2018 Institute of Food Technologists®
Advanced methods for meat tenderization . . .
Shockwave or hydrodynamic-pressure processing is a novel
technology for improving the tenderness of fresh cuts of meat
and utilizes high-pressure shock waves generated by detonation of
small amounts of high energy explosives (electrodetonative) or by
electrical discharge of high voltage between two electrodes (elec-
trohydraulic) under water. Shockwaves are mechanical pressure
pulses which propagate through the meat and induce a “rupture
effect” that tears the muscle structure due to the dissipation of me-
chanical stress at the boundaries of acoustic impedances (Bolumar,
Bindricha, Toepfl, Toldra, & Heinz, 2014). This tenderization
effect (“rupture effect”) causes instantaneous softening of meat,
although accelerated maturation of meat has also been reported
(Bolumar, Enneking, Toepfl, & Heinz, 2013). The use of hydro-
dynamic pressure in food processing has been mainly described for
meat tenderization up to now, and this process of tenderization
has been reported as low-cost and non-invasive with no negative
impact on the chemical and microbial stability of meat (Bolumar
et al., 2014).
Hydrodynamic pressure has been reported to result in a 10% to
70% reduction in shear force depending upon several factors such
as treatment conditions, animal species and muscles, rigor stage,
aging time, muscle-fiber orientation, and background toughness
(Solomon, Liu, Patel, Paroczay, & Eastridge, 2004; 2008; 2011;
Zuckerman, Bowker, Eastridge, & Solomon, 2013; Bolumar et al.,
2014). The mechanisms behind the hydrodynamic tenderization
process have been mainly attributed to the instantaneous impact
of the shockwaves on the meat microstructure causing changes
in muscle cell integrity (Claus, 2002). Shockwaves have been re-
ported to disrupt the integrity of the collagen fibril network of
the endomysium in both aged and non-aged samples (Zuckerman
et al., 2013). However, there are also reports about accelerated
or enhanced maturation (Callahan et al., 2002; Heinz, Töpfl,
Schwägele, & Münch, 2011) with the possible involvement of
the direct activation of proteases and/or indirectly facilitating en-
zymatic contact and degradation of muscle protein structure by
physical disruption. Further research is required in the area as the
mechanisms behind accelerated maturation are not fully under-
stood. Table 3 shows the findings of various studies elucidating
the effect of hydrodynamic-pressure processing on tenderness of
different muscles.
Hydrodynamic-pressure processing does not affect the color
properties (L∗ , a∗ ) of fresh meat (Ha, Dunshea, & Warner, 2017),
meat pH (Bowker, Fahrenholz, Paroczay, & Solomon, 2008),
drip loss or flavor-related components (Bolumar & Toepfl, 2016).
Most of the studies (Bowker et al., 2010b, 2011; Callahan, Berry,
Solomon, & Liu, 2006; Liu and others 2006; Schilling, Mar-
riott, Wang, & Solomon, 2003) have shown no significant effect
of shockwave treatment on cook-loss of aged and unaged meat,
however, it has been shown to increase cook-loss in compari-
son to untreated meat (Bowker, Callahan, & Solomon, 2010a;
Ha et al., 2017; Moeller et al., 1999). Although hydrodynamic-
pressure processing could produce remarkable improvements in
the tenderness of the product in a very short treatment time with
low processing costs, there has been no commercial application
of this technology and further research is required to overcome
the existing limitations, such as development of an industrial size
continuous system with a consistent shockwave delivery as well as
prevention of packaging damage during processing (Bolumar &
Toepfl, 2016).
High-pressure processing (HPP) or high-hydrostatic-pressure
processing is a novel non-thermal preservation technique used
to extend the quality and shelf-life of food products with mini-

C 2018 Institute of Food Technologists®
mal effects on the sensory and nutritional characteristics (Marcos,
Aymerich, Garriga, & Arnau, 2013). It uses pressure under isostatic
conditions by means of a liquid transmitter (Simonin, Duranton, &
De Lamballerie, 2012) and distributes pressure uniformly through-
out the food material without changing the shape and dimensions
of food in the packaging (de Alba & others, 2012). The commer-
cial processing units for pasteurization and sterilization of foods
can deliver pressures up to 1,000 MPa (Rendueles et al., 2011).
For HPP, food is typically hermetically sealed in a flexible packag-
ing under a high pressure of 100 to 600 MPa at room temperature
using a liquid transmitter, subjecting the interior and surface of the
food to uniform pressure to achieve pasteurization (Balasubrama-
niam, Martı́nez-Monteagudo, & Gupta, 2015). Pasteurization of
meat and meat products generally uses pressure levels in the range
of 400 to 600 MPa with short processing times of 3 to 7 min at
room temperature (Bajovic, Bolumar, & Heinz, 2012).
Scientists and technologists have shown considerable interest in
applications of HPP in meat processing as a nonthermal preserva-
tion and postpackaging decontamination technology (Scheinberg,
Svoboda, & Cutter, 2014). It has been projected as one of the best
mild processing techniques to improve the microbial stability and
technological quality of meat and muscle foods (Simonin et al.,
2012). HPP can also improve the tenderness of meat and was
first reported by MacFarlane (1973) and MacFarlane & Morton
(1978). The effect of high pressure on tenderness depends on sev-
eral factors, including rigor stage, pressure, temperature, and the
combination of pressure and temperature (Sun & Holley, 2010).
In general, it has been proposed that low pressures (<200 MPa)
improves the tenderness of pre-rigor meat (Sun & Holley, 2010)
by increasing the proteolytic activity. Morton et al. (2017) stud-
ied the effect of HPP treatment at 175 MPa on the tenderness
of hot-boned beef longissimus thoracis muscle. An improvement in
tenderness was observed with 60% lower shear force in HPP-
treated samples after 1 day, similar to the tenderness produced in
steaks chill-aged for 28 days. The study suggested that HPP could
be used to reduce the processing time, space, and labor associated
with traditional aging without compromising the quality of the
product. High pressure damages the membranes of the sarcoplas-
mic reticulum by physically increasing the calcium concentration
in the cytosol (Okamoto, Suzuki, & Ikeuchi, 1995) and causing
intense muscle contractions which, in turn, accelerate postmortem
glycolysis and a rapid decline in pH. The increased calcium levels
may activate the calpain protease system and pressures of 100 to
200 MPa have also been reported to cause the leakage of cathepsins
into the cytosol by destroying the lysosomal membranes (Hugas,
Garriga, & Monfort, 2002; Ohmori, Shigehisa, Taji, & Hayashi,
1991). These effects, along with high pressure, could lead to dis-
ruption of the myofibrillar structure and thus improve tenderness
(Sikes & Warner, 2016).
Improving the tenderness of post-rigor meat with HPP, how-
ever, requires applying the pressures at high temperatures (ࣙ60
°C) as no beneficial effect was observed when pressures are ap-
plied at ambient (25 to 30 °C) temperatures (Bouton, Ford, Harris,
Macfarlane, & O’shea, 1977; Sikes & Warner, 2016). HPP com-
bined with heat has been reported to be very effective for the ten-
derization of post-rigor beef (Sikes & Tume, 2014), sheep (Mcar-
dle, Marcos, Mullen, & Kerry, 2013), pork (Hong, Chun, Lee,
& Choi, 2012), and chicken (Zamri, Ledward, & Frazier, 2006).
Improvement in the tenderness of beef longissimus dorsi treated at
200 MPa above temperatures of 60 °C was reported to be due to
accelerated proteolysis after pressure treatment (Ma & Ledward,
2004). In addition to the increased protease activity, other factors
Vol. 0, 2018 r Comprehensive Reviews in Food Science and Food Safety 9
Advanced methods for meat tenderization . . .
like solubilization of myosin, conversion of titin isomers, depoly-
merization of actin, and enzyme substrate modifications, which
are responsible for changes in meat microstructure, have also been
suggested for the improvement in tenderness (Sikes & Warner,
2016). Table 4 presents the findings of various studies elucidating
the effect of HPP on the tenderness of different muscles. An im-
portant issue with HPP is that it changes the color of fresh meat by
causing an increase in lightness (L∗ ) and a decrease in redness (a∗ )
particularly at pressures >300 Mpa (Ha et al., 2017). This has been
attributed to the denaturation of myoglobin and to the oxidation
of ferrous myoglobin to ferric brown metmyoglobin and leaves
the meat with a cooked appearance (Guillou, Lerasle, Simonin, &
Federighi, 2017).
Shao et al. (2018) studied the effect of ultra-high-pressure treat-
ment (0, 100, 200, 300, 400, and 500 MPa) on the meat properties
of red swamp crayfish. The hardness values of the samples treated
with high-pressure increased with the increase of treatment pres-
sure. An increase in hardness of the samples was also observed
by Ros-Polski, Koutchma, Xue, Defelice, & Balamurugan (2015)
while studying the effect of HPP on white ground chicken meat.
Neto et al. (2015) studied the effect of hydrostatic-pressure pro-
cessing (100 to 400 MPa for 15 min) on the texture and color of
beef longissimus dorsi muscle. A significant reduction in the shear
force of the samples pressurized at 100 and 200 MPa was ob-
served with an increase of up to 21.12% in tenderness of samples
treated at 200 MPa. The samples treated at 300 MPa showed the
shear force values similar to those of control whereas the samples
treated at 400 MPa showed higher shear force values than unpres-
surized control samples. Sikes and Tume (2014) used a single-step
pressure-heat process to produce tender and juicy beef steaks from
meat that would otherwise be tough when cooked. Steaks from
hind-quarter muscles were subjected to application of high pres-
sure (200 MPa) with simultaneous heat treatment at 60, 64, 68,
72, or 76 °C for 20 min. Meat tenderness was improved for the
pressure-heat samples at temperatures above 64 °C and was optimal
at 76 °C.
HPP has not only been reported to decrease the shear force
but has also been demonstrated to improve sensory eating qual-
ity scores and cooking loss (Morton et al., 2017). Although it
has been reported to reduce cooking loss at moderate pressures
(<300 Mpa), pressures >300 Mpa have been observed to increase
cooking losses. HPP has also been reported to decrease lipid stabil-
ity in foods. There appears to be a critical threshold pressure, be-
tween 300 and 500 MPa, that triggers lipid oxidation in foods like
meat and seafood (Medina-Meza, Barnaba, & Barbosa-Cánovas,
2014). Below 300 MPa there seems to be some effect on lipid
oxidation that increases linearly at pressures above 300 MPa, with
marked changes observed between 300 and 400 MPa in meat,
particularly in pork (Cheah & Ledward, 1995, 1996, 1997). The
pressure required to initiate lipid changes in beef seems to be
lower (200 MPa) than that required for pork and chicken (Ma,
Ledward, Zamri, Frazier, & Zhou, 2007). No effect was observed
on lipid degradation in chicken up to 500 MPa, whereas an oxi-
dation extent statistically equal to heat treatment at 80 °C was in-
duced at 800 MPa (Omana, Plastow, & Betti, 2011; Rivas-Cañedo,
Fernández-Garcı́a, & Nuñez, 2009; Wiggers, Kröger-Ohlsen, &
Skibsted, 2004). Formation of lipid-derived aldehydes, such as
hexanal, pentanal, heptanal, and nonanal, which are responsible
for off-flavors, has been reported to be enhanced by HPP process-
ing in dry-cured ham (Fuentes, Ventanas, Morcuende, Estévez, &
Ventanas, 2010). Pressure-induced breakdown of cell membranes
causing liberation of radicals or precursors of radicals is considered
10 Comprehensive Reviews in Food Science and Food Safety r Vol. 0, 2018
as one of the major causes behind HPP-induced lipid oxidation
(Medina-Meza et al., 2014). Kruk et al. (2011) observed a signif-
icant reduction in flavor, aroma strength, and juiciness of chicken
breast fillets treated at 300 MPa. Increasing pressure was reported
to increase cooking loss and color by increasing L∗ , a∗ , and b∗
values. Pressure of 450 and 600 MPa induced higher lipid oxi-
dation in the samples. No effect of HPP treatment was observed
on the lipid and protein oxidation of sliced dry cured shoulders
from Iberian pigs by Amaro-Blanco, Delgado-Adámez, Martı́n,
and Ramı́rez (2018). HPP did not change the color and sensory
parameters of the shoulders.
Defined as sound waves with frequencies higher than those that
can be detected by the human ear (20 kHz), ultrasound is an
innovative and emerging technology which has the potential to
speed up processes without affecting the quality of foods (Alarcon-
Rojo, Janacua, Rodriguez, Paniwnyk, & Mason, 2015). It has ap-
plications in both the modification and the analysis of foods and
is considered as a sustainable ‘‘green and innovative’’ technique
which typically involves less energy, water, and time (Chemat &
others, 2011). Although it is used in the food industry as a non-
destructive processing technique, low-frequency (20 to 100 kHz)
and high-intensity (10 to 1000 W/cm) ultrasound, also known as
power-ultrasound, can be used to modify or disrupt cell mem-
branes and structures or accelerate certain chemical reactions, and
thus it finds application in the meat industry where it can help in
marinating, curing, drying, and tenderization. Many studies have
reported the potential of application of power-ultrasound for ten-
derization of meat (Jayasooriya, Torley, D’arcy, & Bhandari, 2007;
Terefe, Sikes, & Juliano, 2016), and increased tenderness has been
reported in beef (Stadnik & Dolatowski, 2011), cobia (Chang &
Wong, 2012), squid (Hu et al., 2014), and chicken (Chen et al.,
2015).
The efficacy of ultrasound in improving the tenderness of meat
depends on several factors like species, muscle type, and ultra-
sound conditions (frequency and intensity). Several workers have
studied the effect of ultrasound on post-rigor meat and have re-
ported an improvement in tenderness, with probable mechanisms
of physical disruption in the muscle microstructure by cavitation
and/or release and activation of proteolytic enzymes (Jayasooriya,
Bhandari, Torley, & D’Arey, 2004; Roncales et al., 1993). Ultra-
sonic treatments have been reported to improve the disruption of
myofibrillar structures and to increase proteolysis of chicken meat
by triggering an apoptosis cascade (Chen et al., 2015). Power-
ultrasound has also been reported to reduce muscle fiber diameter
and thermal stability of collagen in beef and suggested hypothesis
by the authors was that improvement in tenderness was the effect
of ultrasound on collagen characteristics (Chang, Xu, Zhou, Li,
& Huang, 2012). Several studies conducted on the use of low-
intensity ultrasound have reported no beneficial effect on meat
tenderization (Lyng, Allen, & Mckenna, 1997, 1998; Sikes, Maw-
son, Stark, & Warner, 2014) indicating the importance of the
intensity when using ultrasound.
Power-ultrasound can accelerate tenderization in pre-rigor meat
and has been suggested to act by accelerating the glycolysis process
by increasing the release of calcium in the cytosol by damaging
the membranes. Although no positive effect was observed on ten-
derness of pre-rigor beef semimembranosus, changes in the Z-line
structure, a delay in rigor onset, and an increased release of calcium
were reported by Got et al. (1999). Sikes et al. (2014) also observed
the effects on metabolism with no improvement in tenderness of
the pre-rigor beef semimembranosus muscle, indicating the potential
of the process for the treatment of DFD (dark, firm, and dry) meat

C 2018 Institute of Food Technologists®
Advanced methods for meat tenderization . . .
by metabolic process modifications (Terefe et al., 2016). Ozuna,
Puig, Garcı́a-Pérez, Mulet, and Cárcel (2013) studied the effect
of high-intensity ultrasound on the textural properties of brined
pork longissimus dorsi muscle. The application of ultrasound in-
creased the hardness of muscle during brining and the effect of
ultrasound on the meat texture was linked to the intensification of
NaCl transport that provoked structural changes in meat proteins.
Pulsed ultrasound has been observed to affect the tertiary and qua-
ternary structure not the primary structure of chicken myofibrillar
proteins (Wang, Yang, Tang, Ni, & Zhou, 2017b).
Table 5 presents findings of various studies elucidating the effect
of ultrasound on the tenderness of different muscles. Although
some authors failed to confirm the tenderizing effect of ultra-
sound, others assert that prolonged exposure to high-intensity ul-
trasound waves causes a significant tenderization of meat. Barekat
and Soltanizadeh (2017) studied the effect of ultrasound (20 kHz)
at power of 100 and 300 W for 10, 20, and 30 min on beef
longissimus lumborum in the presence and absence of 0.1% papain
enzyme solution. Ultrasound caused a significant reduction in
Warner-Bratzler shear force and the reduction was attributed to
the fragmentation of myofibrillar proteins due to the activities
of endogenous and exogenous proteolytic enzymes, disruption of
connective tissues, and physical disruption of meat structure by
cavitation process. Technically, ultrasound can act in two ways
in meat tissues, that is by promoting enzymatic reactions and by
breaking the integrity of muscle cells (Alarcon-Rojo et al., 2015).
Wang et al. (2018) studied the effect of ultrasound on calpain
activity, protein degradation and microstructure of beef semitendi-
nosus muscle. Significantly greater intensities of autolyzed 76 kDa
subunits and the lower intensity of intact 80 kDa form were ob-
served in ultrasound-treated samples at 1 day of storage. Increased
proteolysis was reported in ultrasound treated samples during the
postmortem storage as reflected by an increased degradation of
troponin-T and desmin. These results indicated that ultrasound
treatment could be used to improve the tenderness of beef by
regulating the protein degradation and calpain activation during
post-mortem aging.
Zou et al. (2018) studied the effect of low-frequency ultra-
sonication on the tenderization pattern of goose breast muscle.
Samples treated with ultrasound (20 kHz) at 800 W for 20 min
showed a greater improvement in tenderness during 0 to 24 hr
storage time (4 °C). Significantly higher myofibrillar fragmenta-
tion indices were observed in ultrasonicated meat (22.7%) after
24 hr of storage in comparison to the control (18.2%). The lowest
shear force was obtained in ultrasonicated meat (1970 g) compared
to the control (2,470 g) at 12 hr storage. Ultrasound treatment also
significantly decreased the ATPase activity of actomyosin and in-
creased the count of free actin during storage. Kang, Gao, Ge,
Zhou, and Zhang (2017) studied the effect of ultrasound on the
structure and protein degradation and modification of beef longis-
simus dorsi muscle during curing. A significant increase was ob-
served in the tenderness of the muscle and this was suggested to be
due to increased myofibrillar fragmentation indices and proteolysis
of desmin and troponin-T.
Ultrasound has been reported to increase the cooking yield and
water-holding capacity (Turantaş, Kılıç, & Kılıç, 2015), however, it
has also been reported to increase the lipid oxidation compared to
static brining (Kang et al., 2016). The authors suggested ultrasound
may contribute to protein oxidation by increasing the protein ag-
gregation through disulfide crosslinking (Kang et al., 2016). It may
also change the protein structure in fresh beef as they found an
increase in free sulfhydryl residues and protein surface hydropho-

C 2018 Institute of Food Technologists®
bicity. Although ultrasound has been demonstrated not to affect
the primary structure of chicken myofibrillar proteins (Wang et al.,
2017b), it has been observed to induce changes in the secondary
structure of chicken myofibrillar proteins and disrupt its tertiary
and quaternary structure (Wang et al., 2017b). Low-frequency and
high-power ultrasound have been shown to decrease yellowness,
muscle fiber diameter, and the filtering residues of meat (Chang
et al., 2012). Application of high-frequency ultrasound to pre-
rigor beef has been shown to have the potential for modifying
ATP turnover (Sikes et al., 2014).
Chemical interventions
Salts, organic acids, and phosphates can be incorporated in
meats through immersion, injection, or marination and have well-
established effects on tenderness (Berge et al., 2001). These chem-
icals improve the tenderness of meat by affecting the structure of
the muscle by modifying the protein solubility or mediating it
through the action of proteases. Processes like vascular infusion
have become the commercial reality and several infusion mixes
have come up with promising results.
Marination improves the tenderness, flavor, and value of meat
(Aktas, Aksu, & Kaya, 2003; Goli, Ricci, Bohuon, Marchesseau,
& Collignan, 2014). Traditional marinades contain oil, season-
ings, sugar, and acidic constituents, including vinegar, wine, or
fruit juices (Oreskovich, Bechtel, McKeith, Novakofski, & Basgall,
1992). The various additives which could be used in marinades
to improve the tenderness are organic acids (mainly acetic, citric,
and lactic) and various salts, including calcium salts (Whipple &
Koohmaraie, 1993), sodium chloride (Goli et al., 2014), phos-
phates (Vote et al., 2000), and ammonium hydroxide (Naveena
et al., 2011). The tenderness improvements have been explained
through various physicochemical mechanisms. The salt and acid
present in the marinade diffuses into the muscle tissues reduc-
ing the pH and resulting in significant hydration of the proteins,
thereby causing swelling and weakening of the muscles and con-
nective tissues (Goli, Bohuon, Ricci, Trystram, & Collignan, 2011;
Kim et al., 2013). The hardness of the connective tissues de-
creases through enzymatic mechanisms in an acidic medium or
through decreased electrostatic interactions between myofibrillar
protein chains (Goli et al., 2011). Improvement in tenderness is
also observed due to increased proteolysis by endogenous pro-
teases and/or the exogenous proteases from fruit juices and due
to increased conversion of collagen to gelatine at low pH dur-
ing cooking. Improvement in the water-holding capacity due to
the addition of salts, including sodium chloride, calcium salts, and
phosphates, also contributes to the tenderness (Baublits, Pohlman,
Brown, & Johnson, 2005; Kim et al., 2013).
Marination in acidic solutions is an effective and proven process
of improving meat tenderness, however, due to the slow penetra-
tion of exogenous acids and other compounds, extended periods
are needed to achieve the full effect of the process. The injec-
tion or infusion of the solution allows more rapid diffusion of the
compounds into the muscles and accelerates the improvement in
tenderness. These methods appear to be feasible ways to manip-
ulate the postmortem tenderization process by changing the rate
of glycolysis, rate and state of contraction, and rate of proteoly-
sis (Lee, Stevenson-Barry, Kauffman, & Kim, 2000). Injection of
either sodium chloride or sodium pyrophosphate into hot-boned
muscles reduced cold-induced toughening with “ionic strength”
as one of the main suggested reasons for improved tenderness
(Stevenson-Barry & Kauffman, 1995). Sodium pyrophosphate and
sodium chloride injection improved tenderness in pre-rigor beef
Vol. 0, 2018 r Comprehensive Reviews in Food Science and Food Safety 11
Advanced methods for meat tenderization . . .
muscles by accelerating activation of calpains (Lee et al., 2000).
Injection or infusion of pyrophosphates increase meat pH and
improve meat quality by assisting solubilization of myosin and in-
creasing uptake and retention of water (Lee et al., 2000). Vascular
infusion at a rate of 10% of live weight with a solution composed
of 0.23% dextrose, 0.21% glycerine, 0.14% phosphates, and 0.1%
maltose has been reported to improve the tenderness of beef and
ovine muscles (Farouk, Price, & Salih, 1992). Lactic acid injection
(0.5 M, 10% [w/w]) reduced the toughness of a collagen-rich beef
muscle (pectoralis profundus) as early as 2 days post mortem and time
of injection (pre- vs. post-rigor) had only a minor influence on
meat texture (Berge et al., 2001). Both the myofibrillar tough-
ness and, to a lesser extent, the background toughness (connective
tissue) were reported to be favorably affected.
Calcium chloride has been the most studied and is probably one
of the most effective tenderizing agents of the solutions and ions
used to accelerate meat tenderization (Gerelt, Rusman, Nishiumi,
& Suzuki, 2005). It has shown an improvement in tenderness
in both pre- and post-rigor muscle tissue (Boleman, Boleman,
Binder, McMillin, & Monlezun, 1995; Kerth and others 1995).
Whether applied through marination (Whipple & Koohmaraie,
1993), injection (Wheeler and others 1993), or infusion of individ-
ual muscles or carcasses (Koohmaraie, Babiker, Schroeder, Merkel,
& Duston, 1988), it has shown promising effects on tenderness
by accelerating the postmortem changes. Calcium-activated enzy-
matic degradation seems to be the major tenderization mechanism,
and salting-in of calcium ions (a nonenzymatic mechanism) ap-
pears to be a minor contribution (Lawrence, Dikeman, Stephens,
Obuz, & Davis, 2003). Chloride salts of calcium have the ability to
increase protein solubility by destabilizing the proteins by increas-
ing the electrostatic interactions between protein molecules and
ionic solutions. Thus, improvement in tenderness is mostly me-
diated through the activation of μ-calpain and m-calpain (Gerelt
et al., 2005; Polidori, Trabalza, Marinucci Fantuz, Renieri, &
Polidori, 2000). Although CaCl2 has proven effective on meat
tenderness, there are certain negative effects on the meat quality
as well. It impairs the color stability by inducing discoloration
and reduces oxidative stability, water-holding capacity, and prod-
uct shelf-life (Bekhit et al., 2005; Bunmee, Jaturasitha, Kreuzer, &
Wicke, 2014; Kerth, Miller, & Ramsey, 1995; Jaturasitha, Thira-
wong, Leangwunta, & Kreuzer, 2004). Gerelt, Ikeuchib, Nishiu-
mic, and Suzuki (2002) reported that dipping of meat in 150 mM
calcium chloride solution after osmotic dehydration can be used to
improve tenderness without adversely affecting other palatability
and quality traits.
Enzymatic interventions
Tenderness of the meat can be improved by degradation of
muscle proteins mediated by enzymes that are exogenous and pur-
posely added like enzymes of plant and microbial origin. Although
intrinsic enzymes are mostly active against myofibrillar proteins,
exogenous enzymes can degrade both myofibrillar and connective
tissue proteins. The problem with exogenous enzymes is regulat-
ing their activity as they can result in an over-tenderized meat and
the production of undesirable flavors (Sullivan & Calkins, 2010).
The use of exogenous proteases to improve meat tenderness
has recently become an increasing focus of interest (Fernández-
Lucas et al., 2017). Some enzymes have the potential to reduce the
amount of detectable connective tissues with minimum degrada-
tion of muscle fibers by controlled proteolysis of targeted proteins.
Plant as well as bacterial and fungal enzymes could be employed for
the purpose (Lantto et al., 2010). The exogenous proteases have
12 Comprehensive Reviews in Food Science and Food Safety r Vol. 0, 2018
the capability of digesting connective tissues as well as muscle pro-
teins (Grzonka, Kasprzykowski, & Wiczk, 2007). Plant enzymes,
like cysteine proteases of the papain family, such as papain from pa-
paya latex, bromelain from pineapple fruit and stem, actinidin from
kiwifruit, and the bacterial collagenase are most widely used and
studied exogenous enzymes (Barekat and Soltanizadeh 2017; Ha,
Bekhit, Carne, & Hopkins, 2012; Pietrasik & Shand, 2011). Ex-
ogenous proteases isolated from ginger rhizome (zingibain), fruits
of Cucumis trigonus Roxb plant, and Asparagus officinalis have also
been characterized (Kim, Hamilton, Guddat, & Overall, 2007a;
Ha, Bekhit, Carne, & Hopkins, 2013). Bromelain, ficin, and pa-
pain from plants and the protease from Bacillis subtilis have been
currently approved by USDA’s Food Safety Inspection Service as
“generally recognized as safe” (GRAS) for improving tenderness.
The capability of exogenous enzymes to improve meat tender-
ness has been demonstrated (Ashie, Sorensen, & Nielsen, 2002;
Ha et al., 2012; Lewis & Luh, 1988) and is attributed to their
potential to disrupt the muscle microstructure and cause myofib-
ril protein degradation (Han, Morton, Bekhit, & Sedcole, 2009;
Naveena, Mendiratta, & Anjaneyulu, 2004). However, many ex-
ogenous enzymes tend to degrade major proteins in the muscles
indiscriminately, due to their broad substrate specificity, which
often leads to extensive degradation of meat microstructure and
affects the flavor and texture (Ashie et al., 2002; McKeith, Brewer,
& Bruggen, 1994). Papain has been reported in several studies to
cause the formation of a mushy texture and off flavors (McKeith
et al., 1994). Similar negative impact on the sensory attributes of
meat can be caused by high concentrations of some non-plant
proteases and generate bitterness in treated meat (Qihe, Guoqing,
Yingchun, & Hui, 2006).
A more controlled tenderizing action of actinidin, a cysteine
protease from kiwifruit, on the myofibrillar structure has been
reported (Aminlari, Shekarforoush, Gheisari, & Golestan, 2009;
Christensen et al., 2009), however, its action on collagen is limited,
which makes it less useful for muscles with high collagen content.
Fresh kiwifruit juice, however, has been recently reported to be
effective in solubilizing connective tissues (Ha et al., 2013), sug-
gesting the potential of this protease in improving the tenderness
of specific cuts of meat. Zhang, Sun, Liu, Li, and Jiang (2017)
reported a reduction in shear force by more than half using the
purified actinidin at a dosage of 0.5 mg/100 g muscle in pork and
rabbit longissimus dorsi muscle. The proteolysis observed following
the application of infusion of kiwifruit juice to lamb was attributed
partly to the activation of calpain 2 (Han et al., 2009). Microbial
collagenases, which are capable of degrading collagen that makes
80% of the connective tissues, an important factor for meat ten-
derness, have been proposed to be an alternative to non-specific
plant proteases (Zhao et al., 2012). However, due to their safety
issues and other undesirable effects, these microbial proteases have
not been successfully utilized for tenderizing meat.
All these plant and microbial proteases which have been stud-
ied and reported for meat tenderization are mesophilic or ther-
mophilic, with 50 to 80 °C as their optimal temperature, and
retain only 10% of their highest activity at 20 °C (Zhao et al.,
2012). These proteases loose most of their activity at room tem-
perature when they are used for tenderizing meat before cooking.
Further, these mesophilic or thermophilic proteases remain stable
even during cooking and may cause over-tenderization (Cronlund
& Woychik, 1986). Thus, an ideal protease intended for meat ten-
derization should retain most of its activity at room temperature
and be easily inactivated at cooking temperatures. Cold-adapted
proteases, which retain relatively high activity at 0 to 30 °C and

C 2018 Institute of Food Technologists®
Advanced methods for meat tenderization . . .
get inactivated at temperatures higher than 50 °C (Chen et al.,
2007; Khan & Sylte, 2009), have been suggested as potential meat
tenderizers. Zhao et al. (2012) reported the use of cold-adapted
collagenolytic protease MCP-01 as a promising meat tenderizer at
low and moderate temperatures. Sun et al. (2018) reported the use
of a novel aspartic protease (RmproA) from Rhizomucor miehei
expressed in Pichia pastoris as a potential tenderising agent in
pork muscles (0.25 and 0.5 mg/100 g muscles). The protease was
demonstrated to have the efficacy similar to that of papain in re-
ducing the shear force values of pork muscles. Table 6 presents the
findings of various studies involving the use of exogenous enzymes
on the tenderness of meat.
Conclusions
Technological interventions like electrical stimulation, suspen-
sion methods, blade tenderization, use of exogenous enzymes, and
aging which are currently applied in the meat industry are effec-
tive in improving tenderness. However, there are some limitations
and disadvantages of using these methods. Emerging tenderization
techniques like hydrodynamic-pressure processing, HPP, PEF, ul-
trasound, SmartStretch , and Pi-Vac Elasto-Pack
TM
R
system pro-
vide some advantages over the applied methods, however, would
require initial capital investments and changes in the meat plant
design. Further, more research is required to optimize the process
parameters for different muscles and cuts before some of these
novel methods could find commercial application in the meat
industry.
References
Aaslyng, M. D., & Meinert, L. (2017). Meat flavour in pork and beef - From
animal to meal. Meat Science, 132, 112–117.
Abdel-Naeem, H. H. S., & Mohamed, H. M. H. (2016). Improving the
physicochemical and sensory characteristics of camel meat burger patties
using ginger extract and papain. Meat Science, 118, 52–60.
Adeyemi, K. D., & Sazili, A. Q. (2014). Efficacy of carcass electrical
stimulation in meat quality enhancement: A review. Asian-Australasian
Journal of Animal Sciences, 27, 447–456.
Ahmet, B. (2014). Effect of bromelain on duck breast meat tenderization. All
Theses. 1929. Retrieved from https://tigerprints.clemson.edu/cgi/
viewcontent.cgi?article=2931&context=all_theses
Ahnstrom, M. L., Hunt, M. C., & Lundström, K. (2012). Effects of pelvic
suspension of beef carcasses on quality and physical traits of five muscles
from four gender-age groups. Meat Science, 90, 528–535.
Aktas, N., Aksu, M. I., & Kaya, M. (2003). The effect of organic acid
marination on tenderness, cooking loss and bound water content of beef.
Journal of Muscle Foods, 14, 181–194.
Alarcon-Rojo, A. D., Janacua, H., Rodriguez, J. C., Paniwnyk, L., & Mason,
T. J. (2015). Power ultrasound in meat processing. Meat Science, 107, 86–93.
Amaro-Blanco, G., Delgado-Adámez, J., Martı́n, M. J., & Ramı́rez, R.
(2018). Active packaging using an olive leaf extract and high-pressure
processing for the preservation of sliced dry-cured shoulders from Iberian
pigs. Innovative Food Science and Emerging Technologies, 45, 1–9.
Aminlari, M., Shekarforoush, S. S., Gheisari, H. R., & Golestan, L. (2009).
Effect of actinidin on the protein solubility, water holding capacity, texture,
electrophoretic pattern of beef, and on the quality attributes of a sausage
product. Journal of Food Science, 74, C221–C26.
Andersen, H. J., Oksbjerg, N., Young, J. F., & Therkildsen, M. (2005).
Feeding and meat quality: A future approach. Meat Science, 70, 543–554.
Arroyo, C., Eslami, S., Brunton, N. P., Arimi, J. M., Noci, F., & Lyng, J. G.
(2015a). An assessment of the impact of pulsed electric fields processing
factors on oxidation, colour, texture, and sensory attributes of turkey breast
meat. Poultry Science, 94, 1088–1095.
Arroyo, C., Lascorz, D., O’Dowd, L., Noci, F., Arimi, J., & Lyng, J. G.
(2015b). Effect of pulsed electric field treatments at various stages during
conditioning on quality attributes of beef longissimus thoracis et lumborum
muscle. Meat Science, 99, 52–59.

C 2018 Institute of Food Technologists®
Ashie, I. N. A., Sorensen, T. L., & Nielsen, P. M. (2002). Effects of papain
and a microbial enzyme on meat proteins and beef tenderness. Journal of
Food Science, 67, 2138–2142.
Bajovic, B., Bolumar, T., & Heinz, V. (2012). Quality considerations with
high pressure processing of fresh and value-added meat products. Meat
Science, 92, 280–289.
Balasubramaniam, V. M., Martı́nez-Monteagudo, S. I., & Gupta, R. (2015).
Principles and application of high pressure-based technologies in the food
industry. Annual review of food science and technology, 6, 435–462.
Barba, F. J., Ahrné, L., Xanthakis, E., Landerslev, M. G., & Orlien, V. (2018).
Innovative technologies for food preservation. In F. J. Barba, A. S. Sant’Ana,
V. Orlien, & M. Koubaa (editors), Innovative technologies for food
preservation-Inactivation of spoilage and pathogenic microorganisms (pp. 25–51).
Cambridge, Masachusetts, USA: Academic Press Elsevier Inc.
Barba, F. J., Grimi, N., & Vorobiev, E. (2014). New approaches for the use of
nonconventional cell disruption technologies to extract potential food
additives and nutraceuticals from microalgae. Food Engineering Reviews, 7,
45–62.
Barekat, S., & Soltanizadeh, N. (2017). Improvement of meat tenderness
by simultaneous application of high-intensity ultrasonic radiation and
papain treatment. Innovative Food Science and Emerging Technologies, 39,
223–229.
Baublits, R. T., Pohlman, F. W., Brown, A. H. Jr, & Johnson, Z. B. (2005).
Effects of sodium chloride, phosphate type and concentration, and pump
rate on beef biceps femoris quality and sensory characteristics. Meat Science, 70,
205–214.
Bekhit, A. E. A., Suwandy, V., Carne, A., van de Ven, R., & Hopkins, D. L.
(2016). Effect of repeated pulsed electric field treatment on the quality of
hot-boned beef loins and topsides. Meat Science, 111, 139–146.
Bekhit, A. E. D., Carne, A., Ha, M., & Franks, P. (2014a). Physical
interventions to manipulate texture and tenderness of fresh meat: A review.
International Journal of Food Properties, 17, 433–453.
Bekhit, A. E. D., Hopkins, D. L., Geesink, G., Bekhit, A. E. D., & Franks, P.
(2014b). Exogenous proteases for meat tenderization. Critical Reviews in
Food Science and Nutrition, 54, 1012–1031.
Bekhit, A. E. D., Ilian, M. A., Morton, J. D., Vanhanan, L., Sedcole, J. R., &
Bickerstaffe, R. (2005). Effect of calcium chloride, zinc chloride, and water
infusion on metmyoglobin reducing activity and fresh lamb color. Journal of
Animal Science, 83, 2189–04.
Bekhit, A. E. D., van de Ven, R., Suwandy, V., Fahri, F., & Hopkins, D. L.
(2014c). Effect of pulsed electric field treatment on cold-boned muscles
on different potential tenderness. Food and Bioprocess Technology, 7, 3136–
3146.
Bekhit, A. E. D. A., Carne, A., Ha, M., & Franks, P. (2014d). Physical
interventions to manipulate texture and tenderness of fresh meat: A review.
International Journal of Food Properties, 17, 433–453.
Berge, P., Ertbjerg, P., Larsen, L. M., Astruc, T., Vignon, X., & Møller, A. J.
(2001). Tenderization of beef by lactic acid injected at different times post
mortem. Meat Science, 57, 347–357.
Bertram, H. C., & Aaslyng, M. D. (2007). Pelvic suspension and fast
post-mortem chilling: Effects on technological and sensory quality of pork:
A combined NMR and sensory study. Meat Science, 76, 524–535.
Bhat, Z. F., Morton, J. D., Mason, S., & Bekhit, A. E. D. (2018). Current and
future prospects for the use of pulsed electric field in the meat industry.
Critical Reviews in Food Science and Nutrition, 1–5. https://doi.org/10.1080/
10408398.2018.1425825
Boleman, S. J., Boleman, S. L., Binder, T. D., McMillin, K. W., &
Monlezun, C. J. (1995). Effect of postmortem time of calcium chloride
injection on beef tenderness and drip, cooking and total loss. Meat Science,
39, 35–41.
Bolumar, T., Bindricha, U., Toepfl, S., Toldra, F., & Heinz, V. (2014). Effect
of electrohydraulic shockwave treatment on tenderness, muscle cathepsin
and peptidase activities and microstructure of beef loin steaks from Holstein
young bulls. Meat Science, 98, 759–765.
Bolumar, T., Enneking, M., Toepfl, S., & Heinz, V. (2013). New
developments in shockwave technology intended for meat tenderization:
Opportunities and challenges. A review. Meat Science, 95, 931–939.
Bolumar, T., & Toepfl, S. (2016). Application of shockwaves for meat
tenderization. In: Innovative food processing technologies (pp. 231–258).
Cambridge, United Kingdom: Woodhead Publishing, Elsevier Ltd.
https://doi.org/10.1016/B978-0-08-100294-0.00009-2
Bouton, P. E., Ford, A. L., Harris, P. V., Macfarlane, J. J., & O’shea, J. M.
(1977). Pressure heat treatment of post-rigor muscle: effects on tenderness.
Journal of Food Science, 42, 132–135.
Vol. 0, 2018 r Comprehensive Reviews in Food Science and Food Safety 13
Advanced methods for meat tenderization . . .
Bowker, B. C., Callahan, J. A., & Solomon, M. B. (2010a). Effects of
hydrodynamic pressure processing on the marination and meat quality of
turkey breasts. Poultry Science, 89, 1744–1749.
Bowker, B. C., Fahrenholz, T. M., Paroczay, E. W., & Solomon, M. B.
(2008). Effect of hydrodynamic pressure processing and aging on
sarcoplasmic proteins of beef strip loins. Journal of Muscle Foods, 19, 175–193.
Bowker, B. C., Liu, M. N., Eastridge, J. S., Callahan, J. A., Paroczay, E. W.,
& Solomon, M. B. (2010b). Effect of post-mortem aging and hydrodynamic
pressure processing on pork loin quality. Journal of Muscle Foods, 21,
379–398.
Bowker, B. C., Schaefer, R. B., Grapperhaus, M. J., & Solomon, M. B.
(2011). Tenderization of beef loins using a high efficiency sparker. Innovative
Food Science and Emerging Technologies, 12, 135–141.
Bruce, H. L., Beilken, S. L., & Leppard, P. (2005). Variation in flavor textural
descriptions of cooked steaks from bovine M. longissimus thoracis et
lumborum from different production and aging regimes. Journal of Food
Science, 70, S309–S316.
Bunmee, T., Jaturasitha, S., Kreuzer, M., & Wicke, M. (2014). Can calcium
chloride injection facilitate the aging-derived improvement in the quality of
meat from culled dairy cows? Meat Science, 96, 1440–1445.
Callahan, J. A., Berry, B. W., Solomon, M. B., & Liu, M. N. (2006).
Hydrodynamic pressure-processed beef semitendinosus muscle using a steel
reflector bowl. Journal of Muscle Foods, 17, 105–113.
Callahan, J. A., Solomon, M. B., Paroczay, E. W., Eastridge, J. S., Pursel, V.
G., & Mitchell, V. G. (2002). Enhancement of pork quality using the
hydrodynamic pressure process. In: Institute of Food Technologists, IFT
Annual Meeting Book of Abstracts (p. 111) (46G-14, Anaheim, CA).
Canto, A. C., Lima, B. R., Cruz, A. G., Lazaro, C. A., Freitas, D. G., Faria, J.
A., Silva, T. P. (2012). Effect of high hydrostatic pressure on the colour and
texture parameters of refrigerated caiman (Caiman crocodilus yacare) tail meat.
Meat Science, 91, 255–260.
Cetin, O., & Topcu, T. (2009). Effects of electrical stimulation on meat
quality in goat carcasses. Journal of Food, Agriculture and Environment, 7,
101–105.
Chang, H. C., & Wong, R. X. (2012). Textural and biochemical properties
of cobia (Rachycentron canadum) sashimi tenderized with the ultrasonic water
bath. Food Chemistry, 132, 1340–1345.
Chang, H. J., Xu, X. L., Zhou, G. H., Li, C. B., & Huang, M. (2012).
Effects of characteristics changes of collagen on meat physicochemical
properties of beef semitendinosus muscle during ultrasonic processing. Food
Bioprocess Tech, 5, 285–297.
Channon, H. A., D’Souza, D. N., & Dunshe, F. R. (2016). Flavour and
juiciness of pork using Monte Carlo simulation methods. Meat Science, 116,
58–66.
Cheah, P. B., & Ledward, D. A. (1995). High-pressure effects on lipid
oxidation. Journal of the American Oil Chemists Society, 72, 1059–1063.
Cheah, P. B., & Ledward, D. A. (1996). High-pressure effects on lipid
oxidation in minced pork. Meat Science, 43, 123–134.
Cheah, P. B., & Ledward, D. A. (1997). Catalytic mechanism of lipid
oxidation following high pressure treatment in pork fat and meat. Journal of
Food Science, 62, 1135–139.
Cheftel, J. C., & Culioli, J. (1997). Effects of high pressure on meat: A
review. Meat Science, 46, 211–236.
Chemat, F., & Zill-e-Huma, K. M. K. (2011). Applications of ultrasound in
food technology: processing, preservation and extraction. Ultrasonics
Sonochem, 18, 813–835.
Chen, L., Feng, X., Zhang, Y., Liu, X., Zhang, W., Li, C., Zhou, G. (2015).
Effects of ultrasonic processing on caspase-3, calpain expression and
myofibrillar structure of chicken during post-mortem aging. Food Chemistry,
177, 280–87.
Chen, X. L., Zhang, Y. Z., Lu, J. T., Xie, B. B., Sun, C. Y., & Guo, B.
(2007). Autolysis of a novel multidomain subtilase-cold-adapted deseasin
MCP-01 is pH-dependent and the surface loops in its catalytic domain, the
linker, and the P proprotein domain are susceptible to proteolytic attack.
Biochemical and Biophysical Research Communications, 358, 704–709.
Christensen, M., Torngren, M. A., Gunvig, A., Rozlosnik, N., Lametsch, R.,
Karlsson, A. H., & Ertbjerg, P. (2009). Injection of marinade with actinidin
increases tenderness of porcine M. biceps femoris and affects myofibrils and
connective tissue. Journal of the Science of Food and Agriculture, 89, 1607–1614.
Clark, P. (2006). Pulsed electric field processing. Food Technology, 60, 66–67.
Claus, J. R., Schilling, J. K., Marriott, N. G., Duncan, S. E., Solomon, M.
B., & Wang, H. (2001). Tenderization of chicken and turkey breasts with
electrically produced hydrodynamic shockwaves. Meat Science, 58, 283–286.
14 Comprehensive Reviews in Food Science and Food Safety r Vol. 0, 2018
Claus, J. R. (2002). Shock treatment- shock waves are an effective tool for
tenderizing meat. Meat and Poultry, 48, 61–63.
Cronlund, A. L., & Woychik, J. H. (1986). Effect of microbial rennets on
meat protein fractions. Agricultural Food and Science, 34, 502–505.
de Alba M, B. D., & Medina, M. (2012). High pressure treatments on the
inactivation of Salmonella enteritidis and the characteristics of beef
carpaccio. Meat Science, 92, 823–828.
Deng, Q., Zinoviadou, K. G., Galanakis, C. M., Orlien, V., Grimi, N.,
Vorobiev, E., Barba, F. J. (2014). The effects of conventional and
non-conventional processing on glucosinolates and its derived forms,
isothiocyanates: extraction, degradation, and applications. Food Engineering
Reviews, 7, 357–381.
Dickens, J. A., Lyon, C. E., & Wilson, R. L. (1991). Effect of ultrasonic
radiation on some physical characteristics of broiler breast muscle and
cooked meat. Poultry Science, 70, 389–396.
Doneva, M., Miteva, D., Dyankova, S., Nacheva, I., Metodieva, P., & Dimov,
K. (2015). Efficiency of plant proteases bromelain and papain on turkey
meat tenderness. Biotechnology in Animal Husbandry, 31, 407–413.
Duranton, F., Simonin, H., Chéret, R., Guillou, S., & De Lamballerie, M.
(2012). Effect of high pressure and salt on pork meat quality and
microstructure. Journal of Food Science, 77, E188–E194.
Dutson, T. R., Smith, G. C., & Carpenter, C. L. (1980). Post-mortem
conditioning of meat. In A. M. Pearson & T. R. Dutson (Eds.), Advances in
meat research (Vol. 1, pp. 45). USA: AVI Publishing Company.
Eikelemboom, G., Smulders, F. J. M., & Ruderus, H. (1985). The effect of
high- and low voltage electrical stimulation on beef quality. Meat Science,
15, 247–254.
Elgasim, E. A., & Kennick, W. H. (1982). Effect of high hydrostatic pressure
on meat microstructure. Food Microstructure, 1, 75–82.
Ellies-Oury, M. P., Cantalapiedra-Hijar, G., Durand, D., Gruffat, D., Listrat,
A., Micol, D., Picard, B. (2016). An innovative approach combining animal
performances, nutritional value and sensory quality of meat. Meat Science,
122, 163–172.
Faridnia, F., Bekhit, A. E. A., Niven, B., & Oey, I. (2014). Impact of
pulsed electric fields and post-mortem vacuum aging on beef longissimus
thoracis muscles. International Journal of Food Science and Technology, 49, 2339–
2347.
Faridnia, F., Bremer, P., Burritt, D. J., & Oey, I. (2016). Effects of pulsed
electric fields on selected quality attributes of beef outside flat (biceps
femoris). T. Jarm & P. Kramar (Eds.), First World Congress on
Electroporation and Pulsed Electric Fields In Biology, Medicine and Food
and Environmental Technologies (WC 2015), IFMBE Proceedings 53, 51.
https://doi.org/10.1007/978-981-287-817-5_12
Faridnia, F., Ma, Q. L., Bremer, P. J., Burritt, D. J., Hamid, N., & Oey, I.
(2015). Effect of freezing as pre-treatment prior to pulsed electric field
processing on quality traits of beef muscles. Innovative Food Science and
Emerging Technologies, 29, 31–40.
Farouk, M. M., Price, J. F., & Salih, A. M. (1992). Post-exsanguination
infusion of ovine carcasses: effect on tenderness indicators and muscle
microstructure. Journal of Food Science, 57, 477–496.
Ferguson, D. M., Bruce, H. L., Thompson, J. M., Egan, A. F., Perry, D., &
Shorthose, W. R. (2001). Factors affecting beef palatability-farmgate to
chilled carcass. Australian Journal of Experimental Agriculture, 41, 879–
891.
Ferguson, D. M., & Warner, R. D. (2008). Have we underestimated the
impact of pre-slaughter stress on meat quality in ruminants? Meat Science, 80,
12–19.
Fernández-Lucas, J., Castañeda, D., & Hormigo, D. (2017). New trends for a
classical enzyme: papain, a biotechnological success story in the food
industry. Trends in Food Science & Technology, 68, 91–101.
Fuentes, V., Ventanas, J., Morcuende, D., Estévez, M., & Ventanas, S. (2010).
Lipid and protein oxidation and sensory properties of vacuum-packaged
dry-cured ham subjected to high hydrostatic pressure. Meat Science, 85,
506–514.
Geesink, G. H., Kuchay, S., Chishti, A. H., & Koohmaraie, M. (2006).
μ-Calpain is essential for post-mortem proteolysis of muscle proteins.
Journal of Animal Science, 84, 2834–2840.
Geesink, G. H., Mareko, M. H. D., Morton, J. D., & Bickerstaffe, R. (2001).
Effects of stress and high voltage electrical stimulation on tenderness of lamb
m. longissimus. Meat Science, 57, 265–271.
Gerelt, B., Ikeuchib, Y., Nishiumic, T., & Suzuki, A. (2002). Meat
tenderization by calcium chloride after osmotic dehydration. Meat Science,
60, 237–244.

C 2018 Institute of Food Technologists®
Advanced methods for meat tenderization . . .
Gerelt, B., Rusman, H., Nishiumi, T., & Suzuki, A. (2005). Changes in
calpain and calpastatin activities of osmotically dehydrated bovine muscle
during storage after treatment with calcium. Meat Science, 70, 55–61.
Goli, T., Bohuon, P., Ricci, J., Trystram, G., & Collignan, A. (2011). Mass
transfer dynamics during the acidic marination of turkey meat. Journal of
Food Engineering, 104, 161–168.
Goli, T., Ricci, J., Bohuon, P., Marchesseau, S., & Collignan, A. (2014).
Influence of sodium chloride and pH during acidic marination on water
retention and mechanical properties of turkey breast meat. Meat Science, 96,
1133–1140.
Gorraiz, C., Beriain, M. J., Chasco, J., & Insausti, K. (2002). Effect of aging
time on volatile compounds, odor, and flavour of cooked beef from
Pirenaica and Friesian bulls and heifers. Journal of Food Science, 67,
L916–L922.
Got, F., Culioli, J., Berge, P., Vignon, X., Astruc, T., Quideau, J. M., &
Lethiecq, M. (1999). Effects of high-intensity high-frequency ultrasound on
aging rate, ultrastructure and some physicochemical properties of beef. Meat
Science, 51, 35–42.
Grossi, A., Bolumar, T., Søltoft-Jensen, J., & Orlien, V. (2014). High-pressure
treatment of brine enhanced pork semitendinosus: effect on microbial
stability, drip loss, lipid and protein oxidation, and sensory properties.
Innovative Food Science and Emerging Technologies, 22, 11–21.
Grunert, K. G., Bredahl, L., & Brunsø, K. (2004). Consumer perception of
meat quality and implications for product development in the meat sector:
A review. Meat Science, 66, 259–272.
Grzonka, Z., Kasprzykowski, F., & Wiczk, W. (2007). Cysteine proteases. In
J. Polaina & A. P. MacCabe (Eds.), Industrial enzymes structure, function and
applications (pp. 181–95). Dordrecht, Netherlands: Springer.
Gudmundsson, M., & Hafsteinsson, H. (2001). Effect of electric field pulses
on microstructure of muscle foods and roes. Trends in Food Science &
Technology, 12, 122–128.
Guillemin, N., Bonnet, M., Jurie, C., & Picard, B. (2011). Functional
analysis of beef tenderness. Journal of Proteomics, 75, 352–365.
Guillou, S., Lerasle, M., Simonin, H., & Federighi, M. (2017). High-pressure
processing of meat and meat products. In Emerging technologies in meat
processing (pp. 37–101). Chicester, West Sussex, UK: John Wiley and Sons
Ltd.
Gursansky, B., O’Halloran, J. M., Egan, A., & Devine, C. E. (2010).
Tenderness enhancement of beef from Bos indicus and Bos taurus cattle
following electrical stimulation. Meat Science, 86, 635–641.
Ha, M., Bekhit, A. E. A., Carne, A., & Hopkins, D. L. (2012).
Characterization of commercial papain, bromelain, actinidin, and zingibain
protease preparations and their activities toward meat proteins. Food
Chemistry, 134, 95–105.
Ha, M., Bekhit, A. E. D., Carne, A., & Hopkins, D. L. (2013).
Characterisation of kiwifruit and asparagus enzyme extracts, and their
activities toward meat proteins. Food Chemistry, 136, 989–998.
Ha, M., Dunshea, F. R., & Warner, R. D. (2017). A meta-analysis of the
effects of shockwave and high-pressure processing on colour and cook loss
of fresh meat. Meat Science, 132, 107–111.
Han, J., Morton, J. D., Bekhit, A. E. D., & Sedcole, J. R. (2009). Pre-rigor
infusion with kiwifruit juice improves lamb tenderness. Meat Science, 82,
324–330.
He, F.-Y., Kim, H.-W., Hwang, K.-E., Song, D.-H., Kim, Y.-J., Ham, Y.-K.,
Kim, C.-J.( (2015). Effect of ginger extract and citric acid on the tenderness
of duck breast muscles. Korean Journal for Food Science of Animal Resources, 35,
721–730.
Hegarty, P. V. J., & Allen, C. E. (1975). Thermal effects on the length of
sarcomeres in muscles held at different tensions. Journal of Food Science, 40,
24–27.
Heinz, V., Töpfl, S., Schwägele, F., & Münch, S. (2011). AiF-15884 N:
Anwendung elektrohydraulischer Stoßwellen zur Desintegration biologischer Gewebe
am Beispiel der Zartmachung von Rindfleisch. Bonn: Forschungskreis der
Ernährungsindustrie e.V. (FEI).
Hong, G. P., Chun, J. Y., Lee, S. K., & Choi, M. J. (2012). Modelization and
optimization of quality characteristics of pork treated with various
hydrostatic pressure conditions. Korean Journal for Food Science of Animal
Resources, 32, 274–284.
Hopkins, D. L., Toohey, E. S., Pearce, K. L., & Richards, I. (2008). Some
important changes in the Australian meat processing industry. Australian
Journal of Experimental Agriculture, 48, 752–756.
Hopkins, D. L. (2004). Tenderizing mechanisms: Mechanical. In C. Devine,
M. Dikeman, & W., Jensen (Eds.), Encyclopedia of meat sciences (Vol. 1).
London, UK: Academic Press, Elsevier.

C 2018 Institute of Food Technologists® Vol. 0, 2018 r Comprehensive Reviews in Food Science and Food Safety 15
Hopkins, D. L. (2014). Tenderising mechanisms: Mechanical. In M.,
Dikeman & C. Devine (Eds.), Encyclopedia of meat science (Vol. 3). London,
UK: Academic Press, Elsevier.
Hopkins, D. L. (2017). The eating quality of meat: II-Tenderness. In F.
Toldra (Ed.), Lawrie’s Meat Science (8th ed., pp 357–381). Cambridge,
United Kingdom: Woodhead Publishing. https://www.sciencedirect.com.
ezproxy.lincoln.ac.nz/science/article/pii/B9780081006948000121
Hu, Y., Yu, H., Dong, K., Yang, S., Ye, X., & Chen, S. (2014). Analysis of
the tenderisation of jumbo squid (Dosidicus gigas) meat by ultrasonic
treatment using response surface methodology. Food Chemistry, 160, 219–
225.
Hugas, M., Garriga, M., & Monfort, J. M. (2002). New mild technologies in
meat processing: high pressure as a model technology. Meat Science, 62,
359–71.
Hutchison, C. L., Mulley, R. C., Wiklund, E., Flesch, J. S., & Sims, K.
(2014). Effect of pelvic suspension on the instrumental meat quality
characteristics of red deer (Cervus elaphus) and fallow deer (Dama dama)
venison. Meat Science, 98, 104–109.
Hwang, I. H., Devine, C. E., & Hopkins, D. L. (2003). The biochemical and
physical effects of electrical stimulation on beef and sheep meat tenderness.
Meat Science, 65, 677–691.
Hwang, I. H., & Thompson, J. M. (2001). The effect of time and type of
electrical stimulation on the calpain system and meat tenderness in beef
longissimus dorsi muscle. Meat Science, 58, 135–144.
Ichinoseki, S., Nishiumi, T., & Suzuki, A. (2006). Tenderizing effect of high
hydrostatic pressure on bovine intramuscular connective tissue. Journal of
Food Science, 71, E276–E281.
Irurueta, M., Cadoppi, A., Langman, L., Grigioni, G., & Carduza, F. (2008).
Effect of aging on the characteristics of meat from water buffalo grown in
the Delta del Paraná region of Argentina. Meat Science, 79,
529–533.
Jaturasitha, S., Thirawong, P., Leangwunta, V., & Kreuzer, M. (2004).
Reducing toughness of beef from Bos indicus draught steers by injection of
calcium chloride: effect of concentration and time postmortem. Meat
Science, 68, 61–69.
Jayasooriya, S. D., Bhandari, B. R., Torley, P., & D’Arey, B. R. (2004). Effect
of high-power ultrasound waves on properties of meat: A review.
International Journal of Food Properties, 7, 301–319.
Jayasooriya, S. D., Torley, P. J., D’arcy, B. R., & Bhandari, B. R. (2007).
Effect of high power ultrasound and aging on the physical properties of
bovine semitendinosus and longissimus muscles. Meat Science, 75, 628–639.
Jeyamkondan, S., Jayas, D. S., & Holley, R. A. (1999). Pulsed electric field
processing of foods: A review. Journal of Food Protection, 62, 1088–1096.
Jones, S. B., Carroll, R. J., & Cavanaugh, J. R. (1977). Structural changes in
heated bovine muscle: A scanning electron microscope study. Journal of Food
Science, 42, 125–131.
Judge, M. D., Reeves, E. S., & Aberle, E. D. (1980). Effect of electrical
stimulation on thermal shrinkage temperature of bovine muscle collagen.
Proceedings of the 26th European Meeting of Meat Research Works,
Colorado, Springs (p. 74).
Kang, D.-C., Gao, X.-Q., Ge, Q.-F., Zhou, G.-H., & Zhang, W.-G. (2017).
Effects of ultrasound on the beef structure and water distribution during
curing through protein degradation and modification. Ultraso Sonochemistry,
38, 317–25.
Kang, D.-C., Zou, Y.-H., Cheng, Y.-P., Xing, L.-J., Zhou, G.-H., &
Zhang, W.-G. (2016). Effects of power ultrasound on oxidation and
structure of beef proteins during curing processing. Ultrasonics Sonochemistry,
33, 47–53.
Karlsson, A., Enfalt, A. C., Essen-Gustavsson, B., Lundstrom, K., Rydhmer,
L., & Stern, S. (1993). Muscle histochemical and biochemical properties in
relation to meat quality during selection for increased lean tissue growth rate
in pigs. Journal of Animal Science, 71, 930–938.
Kerth, C. R., Miller, M. F., & Ramsey, C. B. (1995). Improvement of beef
tenderness and quality traits with calcium chloride injection in beef loins 48
hours post-mortem. Journal of Animal Science, 73, 750–756.
Khan, A. A., Randhawa, M. A., Carne, A., Ahmed, I. A. M., Barr, D., Reid,
M., & Bekhit, A. E. A. (2018). Effect of low and high pulsed electric field
processing on macro- and micro-minerals in beef and chicken. Innovative
Food Science and Emerging Technologies, 45, 273–279.
Khan, A. A., Randhawa, M. A., Carne, A., Ahmed, I. A. M., Barr, D., Reid,
M., & Bekhit, A. E. A. (2017). Effect of low and high pulsed electric field
on the quality and nutritional minerals in cold boned beef M. longissimus et
lumborum. Innovative Food Science and Emerging Technologies, 41, 135–143.
https://doi.org/10.1016/j.ifset.2017.03.002
Advanced methods for meat tenderization . . .
Khan, M. I., Jung, S., Nam, K. C., & Jo, C. (2016). Postmortem aging of
beef with a special reference to the dry aging. Korean Journal for Food Science
of Animal Resources, 36, 159–169.
Khan, M. T., & Sylte, I. (2009). Determinants for psychrophilic and
thermophilic features of metallopeptidases of the M4 family. In Silico
Biology, 9, 105–124.
Kim, H. W., Choi, Y. S., Choi, J. H., Kim, H. Y., Lee, M. A., Hwang, K. E.,
Kim, C. J. (2013). Tenderization effect of soy sauce on beef M. biceps femoris.
Food Chemistry, 139, 597–603.
Kim, M., Hamilton, S. E., Guddat, L. W., & Overall, C. M. (2007a). Plant
collagenase: unique collagenolytic activity of cysteine proteases from ginger.
Biochimica et Biophysica Acta, 1770, 1627–1635.
Kim, Y. J., Lee, E. J., Lee, N. H., Kim, Y. H., & Yamamoto, K. (2007b).
Effects of hydrostatic pressure treatment on the physicochemical,
morphological, and textural properties of bovine semitendinosus muscle. Food
Science and Biotechnology, 16, 49–54.
Klont, R. E., Brocks, L., & Eikelenboom, G. (1998). Muscle fibre type and
meat quality. Meat Science, 49, 219–229.
Koohmaraie, M., Babiker, A. S., Schroeder, A. L., Merkel, R. A., & Duston,
T. R. (1988). Acceleration of postmortem tenderization in ovine carcasses
through activation of Ca2+-dependent proteases. Journal of Food Science, 53,
1638–1641.
Koohmaraie, M., & Geesink, G. H. (2006). Contribution of postmortem
muscle biochemistry to the delivery of consistent meat quality with
particular focus on the calpain system. Meat Science, 74, 34–43.
Kovanen, V., Suominen, H., & Heikkinen, E. (1984). Mechanical properties
of fast and slow skeletal muscle with special reference to collagen and
endurance training. Journal of Biomechanics, 17, 725–735.
Kruk, Z. A., Yun, H., Rutley, D. L., Lee, E. J., Kim, Y. J., & Jo, C. (2011).
The effect of high pressure on microbial population, meat quality and
sensory characteristics of chicken breast fillet. Food Control, 22, 6–12.
Kumar, Y., Patel, K. K., & Kumar, K. (2015). Pulse electric field processing
in food technology. International Journal of Engineering Studies and Technical
Approach, 1, 6–17.
Lana, A., & Zolla, L. (2016). Proteolysis in meat tenderization from the point
of view of each single protein: A proteomic perspective. Journal of Proteomics,
147, 85–97.
Lang, Y., Sha, K., Zhang, R., Xie, P., Luo, X., Sun, B., Liu, X. (2016). Effect
of electrical stimulation and hot boning on the eating quality of Gannan yak
longissimus lumborum. Meat Science, 112, 3–8.
Lantto, R., Kruus, K., Puolanne, E., Honkapää, K., Roininen, K., &
Buchert, J. (2010). In Whitehurst, RJ, van Oort M (editors), Enzymes in
food technology (2nd ed) Blackwell Publishing Ltd.
Lawrence, T. E., Dikeman, M. E., Stephens, J. W., Obuz, E., & Davis, J. R.
(2003). In situ investigation of the calcium-induced proteolytic and
salting-in mechanisms causing tenderization in calcium-enhanced muscles.
Meat Science, 66, 69–75.
Lee, S., Stevenson-Barry, J. M., Kauffman, R. G., & Kim, B. C. (2000).
Effect of ion fluid injection on beef tenderness in association with calpain
activity. Meat Science, 56, 301–310.
Lepetit, J., & Culioli, J. (1992). Mechanical properties of meat. Meat Science,
36, 203–237.
Lewis, D. A., & Luh, B. S. (1988). Application of actinidin from kiwifruit to
meat tenderisation and characterisation of beef muscle protein hydrolysis.
Journal of Food Biochemistry, 12, 147–158.
Li, C., Li, J., Li, X., Hviid, M., & Lundström, K. (2011). Effect of
low-voltage electrical stimulation after dressing on color stability and water
holding capacity of bovine longissimus muscle. Meat Science, 88, 559–
565.
Liu, M. N., Solomon, M. B., Vinyard, B., Callahan, J. A., Patel, J. R., West,
R. L., & Chase, C. C. (2006). Use of hydrodynamic pressure processing and
blade tenderization to tenderize top rounds from Brahman cattle. Journal of
Muscle Foods, 17, 79–91.
Liu, Y., Mao, Y., Liang, R., Zhang, Y., Wang, R., Zhu, L., Luo, X. (2016).
Effect of suspension method on meat quality and ultra-structure of Chinese
Yellow Cattle under 12–18 °C pre-rigor temperature-controlled chilling.
Meat Science, 115, 45–49.
Locker, R. H., & Hagyard, C. J. (1963). A cold shortening effect in beef
muscles. Journal of the Science of Food and Agriculture, 14, 787–793.
Lonergan, S. M., Stalder, K. J., Huff-Lonergan, E., Knight, T. J., Goodwin,
R. N., Prusa, K. J., & Beitz, D. C. (2007). Influence of lipid content on
pork sensory quality within pH classification. Journal of Animal Science, 85,
1074–1079.
16 Comprehensive Reviews in Food Science and Food Safety r Vol. 0, 2018
Lyng, J. G., Allen, P., & Mckenna, B. M. (1997). The influence of high
intensity ultrasound baths on aspects of beef tenderness. J Muscle Foods, 8,
237–249.
Lyng, J. G., Allen, P., & Mckenna, B. M. (1998). The effect on aspects of beef
tenderness of pre- and post-rigor exposure to a high intensity ultrasound
probe. Journal of the Science of Food and Agriculture, 78, 308–314.
Ma, H. J., Ledward, D. A., Zamri, A. I., Frazier, R. A., & Zhou, G. H.
(2007). Effects of high pressure/thermal treatment on lipid oxidation in beef
and chicken muscle. Food Chemistry, 104, 1575–1579.
Ma, H. J., & Ledward, D. A. (2004). High pressure/thermal treatment effects
on the texture of beef muscle. Meat Science, 68, 347–355.
Ma, Q., Hamid, N., Oey, I., Kantono, K., Faridnia, F., Yoo, M., & Farouk,
M. (2016). Effect of chilled and freezing pre-treatments prior to
pulsed-electric-field processing on volatile profile and sensory attributes of
cooked lamb meats. Innovative Food Science and Emerging Technologies, 37,
359–374. https://doi.org/10.1016/j.ifset.2016.04.009
Macfarlane, J. J., & Morton, J. D. (1978). Effects of pressure treatment on the
ultrastructure of striated muscle. Meat Science, 2, 281–288.
Macfarlane, J. J. (1973). Pre-rigor pressurization of muscle: effects on pH,
shear value, and taste panel assessment. Journal of Food Science, 38, 294–298.
Maddock, R. (2008). Mechanical tenderization of beef. Downloaded from:
Retrieved from https://www.beefissuesquarterly.com/CMDocs/
BeefResearch/PE_Fact_Sheets/Mechanical_Tenderization_of_Beef.pdf
Maltin, C., Balcerzak, D., Tilley, R., & Delday, M. (2003). Determinants
of meat quality: Tenderness. The Proceedings of the Nutrition Society, 60,
337–347.
Manohar, J., Gayathri, R., & Vishnupriy, V. (2016). Tenderisation of meat
using bromelain from pineapple extract. International Journal of Pharmaceutical
Sciences, 39, 81–85.
Marcos, B., Aymerich, T., Garriga, M., & Arnau, J. (2013). Active packaging
containing nisin and high-pressure processing as post-processing listericidal
treatments for convenience fermented sausages. Food Control, 30, 325–330.
Marino, R., della Malva, A., & Albenzio, M. (2015). Proteolytic changes of
myofibrillar proteins in Podolian meat during aging: Focusing on
tenderness. Journal of Animal Science, 93, 1376–1387.
Marsh, B. B., & Leet, N. G. (1966). Studies in meat tenderness. III. The
effects of cold shortening on tenderness. Journal of Food Science, 31,
450–459.
Mcardle, R. A., Marcos, B., Mullen, A. M., & Kerry, J. P. (2013). Influence
of HPP conditions on selected lamb quality attributes and their stability
during chilled storage. Innovative Food Science and Emerging Technologies, 19,
66–72.
McDonnell, C. K., Allen, P., Chardonnereau, F. S., Arimi, J. M., & Lyng, J.
G. (2014). The use of pulsed electric fields for accelerating the salting of
pork. LWT-Food Science and Technology, 59, 1054–1060.
McKeith, F. K., Brewer, M. S., & Bruggen, K. A. (1994). Effects of enzyme
applications on sensory, chemical and processing characteristics of beef
steaks and roasts. Journal of Muscle Foods, 5, 149–164.
McKenna, D., Maddock, D., & Savell, J. (2003). Water-holding and color
characteristics of beef from electrically stimulated carcasses. Journal of Muscle
Foods, 14, 33–49.
Medina-Meza, I. G., Barnaba, C., & Barbosa-Cánovas, G. V. (2014). Effects
of high pressure processing on lipid oxidation: A review. Innovative Food
Science and Emerging Technologies, 22, 1–10.
Meek, K. I., Claus, J. R., Duncan, S. E., Marriott, N. G., Solomon, M. B.,
Kathman, S. J., & Marini, M. E. (2000). Quality and sensory characteristics
of selected post-rigor, early deboned broiler breast meat tenderized using
hydrodynamic shock waves. Poultry Science, 79, 126–136.
Melody, J. L., Lonergan, S. M., Rowe, L. J., Huiatt, T. W., Mayes, M. S., &
Huff-Lonergan, E. (2004). Early post-mortem biochemical factors influence
tenderness and water holding capacity of three porcine muscles. Journal of
Animal Science, 82, 1195–1205.
Mennecke, B. E., Townsend, A. M., Hayes, D. J., & Lonergan, S. M. (2007).
A study of the factors that influence consumer attitudes toward beef
products using the conjoint market analysis tool. Journal of Animal Science,
85, 2639–2659.
Miller, M. F., Carr, M. A., Ramsey, C. B., Crockett, K. L., & Hoover, L. C.
(2001). Consumer thresholds for establishing the value of beef tenderness.
Journal of Animal Science, 79, 3062–3068.
Moeller, S., Wulf, D., Meeker, D., Ndife, M., Sundararajan, N., & Solomon,
M. B. (1999). Impact of the hydrodyne process on tenderness, microbial
load, and sensory characteristics of pork longissimus muscle. Journal of Animal
Science, 77, 2119–2123.

C 2018 Institute of Food Technologists®
Advanced methods for meat tenderization . . .
Morton, J. D., Bhat, Z. F., & Bekhit, A. E. D. (2018). Proteases and meat
tenderization. In Encyclopaedia of food chemistry. Elsevier Ltd, Amsterdam.
https://doi.org/10.1016/B978-0-12-814026-0.21663-6
Morton, J. D., Bickerstaffe, R., Kent, M. P., Dransfield, E., & Keeley, G. M.
(1999). Calpain-calpastatin and toughness in M. longissimus from electrically
stimulated lamb and beef carcasses. Meat Science, 52, 71–79.
Morton, J. D., Pearson, R. G., Lee, H. Y. Y., Smithson, S., Mason, S. L., &
Bickerstaffe, R. (2017). High-pressure processing improves the tenderness
and quality of hot-boned beef. Meat Science, 133, 69–74.
Mullena, A. M., Álvareza, C., Zeugolisb, D. I., Henchiond, M., O’Neille, E.,
& Drummond, L. (2017). Alternative uses for co-products: Harnessing the
potential of valuable compounds from meat-processing chains. Meat Science,
132, 90–98. https://doi.org/10.1016/j.meatsci.2017.04.243
Nadzirah, K. Z., Zainal, S., Noriham, A., & Normah, I. (2016). Application
of bromelain powder produced from pineapple crowns in tenderising beef
round cuts. International Food Research Journal, 23, 1590–1599.
Naveena, B. M., Kiran, M., Reddy, K. S., Ramakrishna, C., Vaithiyanathan,
S., & Devatkal, S. K. (2011). Effect of ammonium hydroxide on
ultrastructure and tenderness of buffalo meat. Meat Science, 88, 727–732.
Naveena, B. M., Mendiratta, S. K., & Anjaneyulu, A. S. R. (2004).
Tenderisation of buffalo meat using plant proteases from Cucumis trigonus
Roxb (Kachri) and Zingiber officinale roscoe (ginger rhizome). Meat Science, 68,
363–369.
Neto, O. C., Rosenthal, A., Deliza, R., Torrezan, R., Ferreira, J. C. S., Leal
Jr, W. F., & Gaspar, A. (2015). Effects of hydrostatic pressure processing on
texture and color of zebu beef. Food and Bioprocess Technology, 8, 837–843.
Obuz, E., Dikeman, M. E., & Loughin, T. M. (2003). Effects of cooking
method, reheating, holding time, and holding temperature on beef
longissimus lumborum and biceps femoris tenderness. Meat Science, 65, 841–
851.
O’Dowd, L. P., Arimi, J. M., Noci, F., Cronin, D. A., & Lyng, J. G. (2013).
An assessment of the effect of pulsed electrical fields on tenderness and
selected quality attributes of post rigor beef muscle. Meat Science, 93,
303–309.
Offer, G., Knight, P., Jeacocke, R., Almond, R., Cousins, T., Elsey, J.,
Purslow, P. (1989). The structural basis of water holding, appearance and
toughness of meat and meat products. Food Microstructure, 8, 151–170.
Ohmori, T., Shigehisa, T., Taji, S., & Hayashi, R. (1991). Effect of
high-pressure on the protease activities in meat. Agricultural and Biological
Chemistry, 55, 357–361.
Okamoto, A., Suzuki, A., & Ikeuchi, Y. M. S. (1995). Effects of
high-pressure treatment on Ca2+ release and Ca2+ uptake of sarcoplasmic
reticulum. Bioscience, Biotechnology, and Biochemistry, 59, 266–270.
Omana, D. A., Plastow, G., & Betti, M. (2011). The use of β-glucan as a
partial salt replacer in high-pressure-processed chicken breast meat. Food
Chemistry, 129, 768–776.
Oreskovich, D. C., Bechtel, P. J., McKeith, F. K., Novakofski, J., & Basgall,
E. J. (1992). Marinade pH affects textural properties of beef. Journal of Food
Science, 57, 305–311.
Ozuna, C., Puig, A., Garcı́a-Pérez, J. V., Mulet, A., & Cárcel, J. A. (2013).
Influence of high intensity ultrasound application on mass transport,
microstructure and textural properties of pork meat (longissimus dorsi) brined
at different NaCl concentrations. Journal of Food Engineering, 119, 84–93.
Pal, M. (2017). Pulsed electric field processing: An emerging technology for
food preservation. Journal of Experimental Food Chemistry, 3, 2.
Piao, M. Y., Jo, C., Kim, H. J., Lee, H. J., Kim, H. J., Ko, J. Y., & Baik, M.
(2015). Comparison of carcass and sensory traits and free amino acid
contents among quality grades in loin and rump of Korean cattle steers.
Asian-Australasian Journal of Animal Sciences, 28, 1629–1640.
Picard, B., & Gagaoua, M. (2017). Proteomic investigations of beef
tenderness. In M. L. Colgrave (Ed.), Proteomics in food science from farm to fork
(pp. 177–197). Cambridge, Massachusetts, USA: Academic Press. Retrieved
from https://doi-org.ezproxy.lincoln.ac.nz/10.1016/B978-0-12-804007-
2.00011-4
Pietrasik, Z., & Shand, P. J. (2004). Effect of blade tenderization and
tumbling time on the processing characteristics and tenderness of injected
cooked roast. Meat Science, 66, 871–879.
Pietrasik, Z., & Shand, P. J. (2011). Effects of moisture enhancement, enzyme
treatment, and blade tenderization on the processing characteristics and
tenderness of beef semimembranosus steaks. Meat Science, 88, 8–13.
Pillet, F., Formosa-Dague, C., Baaziz, H., Dague, E., & Rols, M.-P. (2016).
Cell wall as a target for bacteria inactivation by pulsed electric fields.
Scientific Reports, 6, 19778.

C 2018 Institute of Food Technologists® Vol. 0, 2018 r Comprehensive Reviews in Food Science and Food Safety 17
Pohlman, F. W., Dikeman, M. E., & Zayas, J. F. (1997). The effect of low
intensity ultrasound treatment on shear properties, color stability and
shelf-life of vacuum-packaged beef semitendinosus and biceps femoris muscles.
Meat Science, 45, 329–337.
Polidori, P., Ariani, A., Micozzi, D., & Vincenzetti, S. (2016). The effects of
low voltage electrical stimulation on donkey meat. Meat Science, 119,
160–164.
Polidori, P., Lee, S., Kauffman, R. G., & Marsh, B. B. (1999). Low voltage
electrical stimulation of lamb carcasses: Effects on meat quality. Meat Science,
53, 179–182.
Polidori, P., Trabalza, M., Marinucci Fantuz, F., Renieri, C., & Polidori, F.
(2000). Tenderization of wether lambs meat through pre-rigor infusion of
calcium ions. Meat Science, 55, 197–200.
Puértolas, E., & Barba, F. J. (2016). Electrotechnologies applied to
valorization of by-products from food industry: Main findings, energy and
economic cost of their industrialization. Food Bioproducts Process, 100,
172–184.
Puertolas, E., Saldana, G., Condon, S., Alvarez, I., & Raso, J. (2010).
Evolution of polyphenolic compounds in red wine from Cabernet Sauvignon
grapes processed by pulsed electric fields during aging in bottle. Food
Chemistry, 119, 1063–1070.
Qihe, C., Guoqing, H., Yingchun, J., & Hui, N. (2006). Effects of elastase
from a Bacillus strain on the tenderization of beef meat. Food Chemistry, 98,
624–629.
Ramezani, R., Aminlari, M., & Fallahi, H. (2003). Effect of chemically
modified soy proteins and ficin-tenderized meat on the quality attributes of
sausage. Journal of Food Science, 68, 85–88.
Renand, G., Picard, B., Touraille, C., Berge, P., & Lepetit, J. (2001).
Relationships between muscle characteristics and meat quality traits of
young Charolais bulls. Meat Science, 59, 49–60.
Rendueles, E., Omer, M. K., Alvseike, O., Alonso-Calleja, C., Capita, R., &
Prieto, M. (2011). Microbiological food safety assessment of high
hydrostatic pressure processing: A review. LWT-Food Science and Technology,
44, 1251–1260.
Rhee, M., Wheeler, T., Shackelford, S., & Koohmaraie, M. (2004). Variation
in palatability and biochemical traits within and among eleven beef muscles.
Journal of Animal Science, 82, 534.
Rivas-Cañedo, A., Fernández-Garcı́a, E., & Nuñez, M. (2009). Volatile
compounds in fresh meats subjected to high-pressure processing: Effect of
the packaging material. Meat Science, 81, 321–328.
Roncales, P. (1993). Ultrasonification of lamb skeletal muscle fibres enhances
post-mortem proteolysis. Zeitschrift Fuer Lebensmittel-Untersuchung Und-
Forschung, 78, 308–314.
Ros-Polski, V., Koutchma, T., Xue, J., Defelice, C., & Balamurugan, S.
(2015). Effects of high-hydrostatic-pressure processing parameters and NaCl
concentration on the physical properties, texture and quality of white
chicken meat. Innovative Food Science and Emerging Technologies, 30, 31–42.
Saldaña, G., Álvarez, I., Condón, S., & Raso, J. (2014). Microbiological
aspects related to the feasibility of PEF technology for food pasteurization.
Critical Reviews in Food Science and Nutrition, 54, 1415–1426.
Sampedro, F., McAloon, A., Yee, W., Fan, X., & Geveke, D. J. (2014). Cost
analysis and environmental impact of pulsed electric fields and high-pressure
processing in comparison with thermal pasteurization. Food and Bioprocess
Technology, 7, 1928–1937.
Sánchez, E., Pérez, C., Barreras, A., Figueroa, F., & Herrera, B. (2016).
Quantifying the differential effect that the electrical stimulation of bovine
carcasses has on pH and colour. Veterinarski Arhiv, 86, 149–158.
Scheinberg, J. A., Svoboda, A. L., & Cutter, C. N. (2014). High-pressure
processing and boiling water treatments for reducing Listeria monocytogenes,
Escherichia coli O157: H7, Salmonella spp., and Staphylococcus aureus during
beef jerky processing. Food Control, 39, 105–110.
Schenkova, N., Sikulova, M., Jelenikova, J., Pipek, P., Houska, M., & Marek,
M. (2007). Influence of high-hydrostatic pressure and papain treatment on
the quality of beef meat. High Pressure Generation, 27, 163–168.
Schilling, M. W., Claus, J. R., Marriot, N. G., Solomon, M. B., Eigel, W. N.,
& Wang, H. (2002). No effect of hydrodynamic shock wave on protein
functionality of beef muscle. Journal of Food Science, 67, 335–340.
Schilling, M. W., Marriott, N. G., Wang, H., & Solomon, M. B. (2003).
Characteristics of USDA utility cow beef subjected to blade
tenderization and hydrodynamic shock waves. Journal of Muscle Foods, 14,
131–142.
Shao, Y., Xiong, G., Ling, J., Hu, Y., Shi, L., Qiao, Y., Wang, L. (2018).
Effect of ultra-high-pressure treatment on shucking and meat properties of
Advanced methods for meat tenderization . . .
red swamp crayfish (Procambarus clarkia). LWT - Food Science and Technology,
87, 234–240.
Sikes, A. L., Mawson, R., Stark, J., & Warner, R. (2014). Quality properties
of pre- and post-rigor beef muscle after interventions with high frequency
ultrasound. Ultrasonics Sonochemistry, 21, 2138–2143.
Sikes, A. L., & Tume, R. K. (2014). Effect of processing temperature on
tenderness, colour and yield of beef steaks subjected to high-hydrostatic
pressure. Meat Science, 97, 244–248.
Sikes, A. L., & Warner, R. (2016). Application of high hydrostatic pressure
for meat tenderization. In K. Knoerzer, P. Juliana, & G. Smithers (Eds.),
Innovative food processing technologies (pp. 259–290). Cambridge, UK:
Woodhead Publishing. https://doi.org/10.1016/B978-0-08-100294-
0.00010-9
Silva, T. J. P., Orcutt, M. V., Forrest, J. C., Bracker, C. E., & Judge, M. D.
(1993). Effect of heating rate on shortening, ultrastructure and fracture
behaviour of pre-rigor beef muscle. Meat Science, 33, 1–24.
Simmons, N. J., Daly, C. C., Cummings, T. L., Morgan, S. K., Johnson, N.
V., & Lombard, A. (2008). Reassessing the principles of electrical
stimulation. Meat Science, 80, 110–122.
Simonin, H., Duranton, F., & De Lamballerie, M. (2012). New insights into
the high-pressure processing of meat and meat products. Comprehensive
Reviews in Food Science and Food Safety, 11, 285–306.
Sitz, B. M., Calkins, C. R., Feuz, D. M., Umberger, W. J., & Eskridge, K.
M. (2006). Consumer sensory acceptance and value of wet-aged and
dry-aged beefsteaks. Journal of Animal Science, 84, 1221–1226.
Smit, N. R., Summerfield, J. W., & Cannon, J. E. (2010). Use of high
pressure processing to improve muscle quality by inhibiting post-mortem
glycolysis. WO 2010/022305, Retrieved from https://www.google.com/
patents/US20100048116
Smith, M. A., Bush, R. D., van de Ven, R. J., & Hopkins, D. L. (2017). The
combined effects of grain supplementation and tenderstretching on alpaca
(Vicugna pacos) meat quality. Meat Science, 125, 53–60.
Smith, N. B., Cannon, J. E., Novakofsky, J. E., Mckeith, F. K., & O’brien,
W. D. J. (1991). Tenderization of semitendinosus muscle using high intensity
ultrasound. In Proceedings of the ultrasonics symposium, Lake Beuna Vista,
Florida.
Smith, R. D., Nicholson, K. L., Nicholson, J. D. W., Harris, K. B., Miller,
R. K., Griffin, D. B., & Savell, J. W. (2008). Dry versus wet aging of beef:
Retail cutting yields and consumer palatability evaluations of steaks from US
choice and US select short loins. Meat Science, 79, 631–639.
Solomon, M. B., Carpenter, C. E., Snowder, G. D., & Cockett, N. E.
(1998). Tenderizing callipyge lamb with the hydrodyne process and
electrical stimulation. Journal of Muscle Foods, 9, 305–311.
Solomon, M. B., Liu, M., Patel, J., Paroczay, E., & Eastridge, J. (2004).
Tenderness improvement in fresh and frozen/thawed beef strip loins treated
with hydrodynamic-pressure processing. Journal of Animal Science, 82, 18–22.
Solomon, M. B., Liu, M. N., Patel, J., Paroczay, E., Eastridge, J., &
Coleman, S. W. (2008). Tenderness improvement in fresh or frozen/thawed
beef steaks treated with hydrodynamic-pressure processing. Journal of Muscle
Foods, 19, 98–109.
Solomon, M. B., Long, J. B., & Eastridge, J. S. (1997). The hydrodyne: A
new process to improve beef tenderness. Journal of Animal Science, 75,
1534–1537.
Solomon, M. B., Sharma, M., & Patel, J. R. (2011). Hydrodynamic pressure
processing of meat products. In H. Q. Zhang, G. V. Barbosa-Canovas, V. M.
Bala Balasubramaniam, C. Patrick Dunne, D. F. Farkas, & J. T. C. Yuan
(Eds.), Non-thermal processing technologies for food (pp. 98–108). New Jersey,
USA: Wiley Blackwell, IFT Press.
Sorheim, O., & Hildrum, K. I. (2002). Muscle stretching techniques for
improving meat tenderness. Trends in Food Science & Amp; Technology, 13,
127–135.
Souza, C. M., Boler, D. D., Clark, D. L., Kutzler, L. W., Holmer, S. F.,
Summerfield, J. W., Killefer, J. (2012). Varying the temperature of the liquid
used for high-pressure processing of prerigor pork: Effects on fresh pork
quality, myofibrillar protein solubility, and frankfurter textural properties.
Journal of Food Science, 77, S54–S61.
Stadnik, J., Dolatowski, Z. J., & Baranowska, H. M. (2008). Effect of
ultrasound treatment on water holding properties and microstructure of beef
(semimembranosus) during aging. LWT-Food Science and Technology, 41,
2151–2158.
Stadnik, J., & Dolatowski, Z. J. (2011). Influence of sonication on
Warner-Bratzler shear force, color, and myoglobin of beef (M.
semimembranosus). European Food Research and Technology, 233, 553–559.
18 Comprehensive Reviews in Food Science and Food Safety r Vol. 0, 2018
Stevenson-Barry, J. M., & Kauffman, R. G. (1995). Tenderization of muscle
via pre-rigor injection of ions. In Proceedings of 41st International Congress of
meat science and technology (pp. 598–599). San Antonio, TX, USA.
Strydom, P. E., & Frylinck, L. (2014). Minimal electrical stimulation is
effective in low stressed and well-fed cattle. Meat Science, 96, 790–798.
Sullivan, G. A., & Calkins, C. R. (2010). Application of exogenous enzymes
to beef muscle of high and low-connective tissue. Meat Science, 85, 730–734.
Sun, Q., Chen, F., Geng, F., Luo, Y., Gong, S., & Jiang, Z. (2018). A novel
aspartic protease from Rhizomucor miehei expressed in Pichia pastoris and its
application on meat tenderization and preparation of turtle peptides. Food
Chemistry, 245, 570–577.
Sun, X. D., & Holley, R. A. (2010). High-hydrostatic-pressure effects on the
texture of meat and meat products. Journal of Food Science, 75, R17–R23.
Suwandy, V., Carne, A., van de Ven, R., Bekhit, A. E. A., & Hopkins, D. L.
(2015a). Effect of pulsed electric field on the proteolysis of cold boned beef
longissimus lumborum and semimembranosus. Meat Science, 100, 222–226.
Suwandy, V., Carne, A., van de Ven, R., Bekhit, A. E. A., & Hopkins, D. L.
(2015b). Effect of pulsed-electric-field treatment on hot-boned muscles of
different potential tenderness. Meat Science, 105, 25–31.
Suwandy, V., Carne, A., van de Ven, R., Bekhit, A. E. A., & Hopkins, D. L.
(2015c). Effect of pulsed electric field treatment on the eating and keeping
qualities of cold-boned beef loins: Impact of initial pH and fiber
orientation. Food and Bioprocess Technology, 8, 1355–1365.
Suwandy, V., Carne, A., van de Ven, R., Bekhit, A. E. A., & Hopkins, D. L.
(2015d). Effect of repeated pulsed-electric-field treatment on the quality of
cold-boned beef loins and topsides. Food and Bioprocess Technology, 8,
1218–1228.
Taylor, A., & Martoccia, L. (1995). The effect of low-voltage and
high-voltage electrical stimulation on pork quality. Meat Science, 39,
319–326.
Taylor, J., Toohey, E. S., van de Ven, R., & Hopkins, D. L. (2013).
SmartStretchTM technology VI. The impact of SmartStretchTM technology
on the meat quality of hot-boned beef striploin (m. longissimus lumborum).
Meat Science, 93, 413–419.
Taylor, J. M., Hopkins, D. L., & van de Ven, R. (2010). The effect of a
meat-stretching device on the tenderness of hot-boned beef topsides and
“rostbiffs”, In: Proceedings of the 56th International Congress of meat science and
technology, Aug. 15–20, 2010, Session E 072 (pp 1–4), Jeju, Korea.
Taylor, J. M., & Hopkins, D. L. (2011). Patents for stretching and shaping
meats. Recent Patents on Food Nutrition Agriculture, 3, 91–101.
Terefe, N. S., Sikes, A. L., & Juliano, P. (2016). Ultrasound for structural
modification of food products. In: K. Knoerzer, P. Juliana, & G. Smithers
(Eds.), Innovative food processing technologies (pp. 209–230). Cambridge, UK:
Woodhead Publishing. https://doi.org/10.1016/B978-0-08-100294-0.
00010-9
Thompson, J. M., Hopkins, D. L., D’Souza, D. N., Walker, P. J., Baud, S. R.,
& Pethick, D. W. (2005). The impact of processing on sensory and objective
measurements of sheep meat eating quality. Australian Journal of Experimental
Agriculture, 45, 561–573.
Thorslund, C. A. H., Sandøe, P., Aaslyng, M. D., & Lassen, J. (2016). A good
taste in the meat, a good taste in the mouth, Animal welfare as an aspect of
pork quality in three European countries. Livestock Sci, 193, 58–65.
Toepfl, S. (2006). Pulsed electric fields (PEF) for permeabilization of cell membranes
in food- and bioprocessing: Applications, process and equipment design and cost
analysis. Published doctoral thesis. Berlin University of Technology,
Germany. Retrieved from https://depositonce.tu-berlin.de/handle/
11303/1738
Toohey, E. S., van de Ven, R., Thompson, J. M., Geesink, G. H., &
Hopkins, D. L. (2012a). SmartStretchTM technology. I. Improving the
tenderness of sheep topsides (m. semimembranosus) using a meat stretching
device. Meat Science, 91, 142–147.
Toohey, E. S., van de Ven, R., Thompson, J. M., Geesink, G. H., &
Hopkins, D. L. (2012b). SmartStretchTM technology. II. Improving the
tenderness of leg meat from sheep using a meat stretching device. Meat
Science, 91, 125–130.
Toohey, E. S., van de Ven, R., Thompson, J. M., Geesink, G. H., &
Hopkins, D. L. (2012c). SmartStretchTM Technology: V. The impact of
SmartStretchTM technology on beef topsides (m. semimembranosus) meat
quality traits under commercial processing conditions. Meat Science, 92,
24–29.
Toohey, E. S., van de Ven, R., Thompson, J. M., Geesink, G. H., &
Hopkins, D. L. (2013). SmartStretchTM technology. III. The impact of
medium-voltage-stimulation and SmartStretchTM technology on sheep

C 2018 Institute of Food Technologists®
Advanced methods for meat tenderization . . .
topside (m. semimembranosus) meat quality traits under commercial
processing conditions. Meat Science, 93, 187–193.
Troy, D. J., & Kerry, J. P. (2010). Consumer perception and the role of
science in the meat industry. Meat Science, 86, 214–226.
Turantaş, F., Kılıç, G. B., & Kılıç, B. (2015). Ultrasound in the meat industry:
General applications and decontamination efficiency. International Journal of
Food Microbiology, 198, 59–69.
Veiseth, E., Shackelford, S., Wheeler, T., & Koohmaraie, M. (2004). Factors
regulating lamb longissimus tenderness are affected by age at slaughter. Meat
Science, 68, 635–640.
Vote, D. J., Platter, W. J., Tatum, J. D., Schmidt, G. R., Belk, K. E., Smith,
G. C., & Speer, N. C. (2000). Injection of beef strip loins with solution
containing sodium tripolyphosphate, sodium lactate, and sodium chloride to
enhance palatability. Journal of Animal Science, 78, 952–957.
Walkling-Ribeiro, M., Rodrı́guez-Gonzalez, O., Jayaram, S. H., & Griffiths,
M. W. (2011). Processing temperature, alcohol and carbonation levels and
their impact on pulsed electric fields (PEF) mitigation of selected
characteristic microorganisms in beer. Food Research International, 44,
2524–2533.
Wang, A., Kang, D., Zhang, W., Zhang, C., Zou, Y., & Zhou, G. (2018).
Changes in calpain activity, protein degradation and microstructure of beef
M. semitendinosus by the application of ultrasound. Food Chemistry, 245,
724–730.
Wang, H., Claus, J. R., & Marriott, N. G. (1994). Selected skeletal alterations
to improve tenderness of beef round muscles. Journal of Muscle Foods, 5,
137–147.
Wang, J. Y., Yang, Y. L., Tang, X. Z., Ni, W. X., & Zhou, L. (2017b). Effects
of pulsed ultrasound on rheological and structural properties of chicken
myofibrillar protein. Ultrasonics Sonochemistry, 38, 225–233.
Wang, L. L., Han, L., Ma, X. L., Yu, Q. L., & Zhao, S. N. (2017a). Effect of
mitochondrial apoptotic activation through the mitochondrial membrane
permeability transition pore on yak meat tenderness during post-mortem
aging. Food Chemistry, 234, 323–331.
Warner, R. D., McDonnell, C., Bekhit, A. E. D., Claus, J., Vaskoska, R.,
Sikes, A., Ha, M. (2017). Systematic review of emerging and innovative
technologies for meat tenderization. Meat Science, 132, 72–89.
https://doi.org/10.1016/j.meatsci.2017.04.241
Wheeler, T., Shackelford, S., & Koohmaraie, M. (2000). Variation in
proteolysis, sarcomere length, collagen content, and tenderness among
major pork muscles. Journal of Animal Science, 78, 958–965.
Wheeler, T. L., Koohmaraie, M., Lansdell, J. L., Siragusa, G. R., & Miller,
M. F. (1993). Effect of postmortem injection time, injection level, and
concentration of calcium chloride on beef quality traits. Journal of Animal
Science, 71, 2965–2974.
Whetstone, S., Adhikari, K., & Chamber, E.-I. V. (2014). Impact of
seasoning and bromelain on sensory attributes of beef steaks. Journal of
Human Nutrition & Food Science, 2, 1023.

C 2018 Institute of Food Technologists®
View publication stats
Whipple, G., & Koohmaraie, M. (1993). Calcium chloride marination effects
on beef steak tenderness and calpain proteolytic activity. Meat Science, 33,
265–275.
White, A., O’Sullivan, A., Troy, D. J., & O’Neill, E. E. (2006). Effects of
electrical stimulation, chilling temperature and hot-boning on the
tenderness of bovine muscles. Meat Science, 73, 196–203.
Wiggers, S. B., Kröger-Ohlsen, M. V., & Skibsted, L. H. (2004). Lipid
oxidation in high-pressure processed chicken breast during chill storage and
subsequent heat treatment: Effect of working pressure, packaging
atmosphere and storage time. European Food Research and Technology, 219,
167–170.
Wiklund, E., Stevenson-Barry, J., Duncan, S., & Littlejohn, R. (2001).
Electrical stimulation of red deer (Cervus elaphus) carcasses - effects on rate
of pH-decline, meat tenderness, colour stability and water-holding capacity.
Meat Science, 59, 211–220.
Wu, W., Fu, Y., Therkildsen, M., Li X, M., & Dai, R. T. (2015). Molecular
understanding of meat quality through application of proteomics. Food
Research International, 31, 13–28.
Xiong, G. Y., Zhang, L. L., Zhang, W., & Wu, J. (2012). Influence of
ultrasound and proteolytic enzyme inhibitors on muscle degradation,
tenderness, and cooking loss of hens during aging. Czech Journal of Food
Science, 30, 195–205.
Young, L. L., Buhr, R. J., & Lyon, C. E. (1999). Effect of polyphosphate
treatment and electrical stimulation on postchill changes in quality of broiler
breast meat. Poultry Science, 78, 267–271.
Zamri, A. I., Ledward, D. A., & Frazier, R. A. (2006). Effect of combined
heat and high-pressure treatments on the texture of chicken breast muscle
(pectoralis fundus). Journal of Agricultural and Food Chemistry, 54, 2992–
2996.
Zhang, B., Sun, Q., Liu, H.-J., Li, S.-Z., & Jiang, Z.-Q. (2017).
Characterization of actinidin from Chinese kiwifruit cultivars and its
applications in meat tenderization and production of angiotensin
I-converting enzyme (ACE) inhibitory peptides. LWT - Food Science and
Technology, 78, 1–7.
Zhao, G. Y., Zhou, M. Y., Zhao, H. L., Chen, X. L., Xie, B. B., Zhang, X.
Y., Zhang, Y. Z. (2012). Tenderization effect of cold-adapted collagenolytic
protease MCP-01 on beef meat at low temperature and its mechanism. Food
Chemistry, 134, 1738–1744.
Zou, Y., Zhang, K., Bian, H., Zhang, M., Sun, C., Xu, W., & Wang, D.
(2018). Rapid tenderizing of goose breast muscle based on actomyosin
dissociation by low-frequency ultrasonication. Process Biochemistry (Barking,
Uk), 65, 115–122.
Zuckerman, H., Bowker, B. C., Eastridge, J. S., & Solomon, M. B. (2013).
Microstructure alterations in beef intramuscular connective tissue
caused by hydrodynamic pressure processing. Meat Science, 95,
603–607.
Vol. 0, 2018 r Comprehensive Reviews in Food Science and Food Safety 19