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Innovative Food Science and Emerging Technologies 21 (2014) 5057

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Innovative Food Science and Emerging Technologies


journal homepage: www.elsevier.com/locate/ifset

Enhanced texture, yield and safety of a ready-to-eat salted duck meat


product using a high pressure-heat process
Muhammad Ammar Khan a,c, Sher Ali a, Muhammad Abid a,d, Hussain Ahmad a,c, Lixia Zhang a,
Ronald Keith Tume b, Guanghong Zhou a,
a
Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Key Laboratory of Animal Products Processing, Ministry of Agriculture, College of Food Science and Technology,
Nanjing Agricultural University, Nanjing 210095, PR China
b
CSIRO, Animal, Food and Health Sciences, Brisbane, Queensland 4108, Australia
c
University College of Agriculture and Environmental Sciences, The Islamia University of Bahawalpur, Pakistan
d
Department of Food Technology, Pir Mehr Ali Shah Arid Agriculture University, Rawalpindi, Pakistan

a r t i c l e

i n f o

Article history:
Received 3 June 2013
Accepted 19 October 2013
Editor Proof Receive Date 15 November 2013
Keywords:
High pressure processing
Cooking
Duck meat
Protein denaturation
NMR proton relaxation

a b s t r a c t
This study investigated the effects of high pressure, in combination with heat, for development of a ready-to-eat
salted duck meat product. Duck breast was subjected to a salting and pickling process prior to either heatingalone (70C) or high-pressure (200MPa) with heating (70C) for 10 or 20min, and compared with a cooked control (core temperature 80C at 0.1MPa) for quality assessment. Compared with the cooked control, pressure-heat
treated samples exhibited reduced cooking losses, and NMR showed they had larger fast-relaxation proton compartments. Pressure-heat preserved some sarcoplasmic and connective tissue proteins, but caused greater denaturation of actin than with heat-only samples. The reduction in microbial load with pressure-heat indicated
suitability of the process for ready-to-eat products. Pressure-heat treatment did not affect color, but there was
a decrease in hardness and gumminess, suggesting higher palatability. The reduction in cooking losses, resulting
from altered proton compartmentalization, and changes in myobrillar proteins enhanced product acceptability.
Industrial relevance: The application of high hydrostatic pressure technology for food processing has gained much
interest over recent decades because of its benets over conventional methods. Its suitability for ready-to-eat
Nanjing-style salted duck meat product was determined by assessment of proton compartmentalization and mobility by NMR, extent of protein denaturation by DSC, microbial numbers, surface color and texture which described product acceptability, palatability and microbial safety. This single-step process will aid the meat
processing industry in improving existing processing methods by incorporation of high pressure technology to
improve product quality and process efciency.
2013 Elsevier Ltd. All rights reserved.

1. Introduction
Processing methods play an important role in determining quality,
safety and acceptability of food products. Meat processing is a complex
process that demands a comprehensive balance between processors'
and consumers' expectations, by demonstrating tangible improvements
of quality and safety at an affordable cost, together with environmental
sustainability. The constant development and improvement of new and
existing products have evolved the meat-processing sector. Based on
processing technologies, meat products are widely classied as raw,
minimally processed and ready-to-eat products. Thermal processing is a
prerequisite for most of the ready-to-eat meat products. It brings about
desirable changes in color, texture, structure and sensory properties,

Corresponding author at: Key Laboratory of Meat Processing and Quality Control,
Ministry of Education, College of Food Science and Technology, Nanjing Agricultural
University, Nanjing 210095, PR China. Tel.: +86 25 84395376; fax: +86 25 84395939.
E-mail addresses: ammar7may@msn.com (M.A. Khan), ghzhou@njau.edu.cn (G. Zhou).
1466-8564/$ see front matter 2013 Elsevier Ltd. All rights reserved.
http://dx.doi.org/10.1016/j.ifset.2013.10.008

mainly resulting from protein denaturation in the food matrix (Moure,


Sineiro, Domnguez, & Paraj, 2006). Knowledge of the core temperature
of meat is important as this allows an estimate of microbial inactivation.
Meat temperatures and heating times are specied to ensure food safety.
Temperatures up to 6065 C are sufcient to bring about desired palatability characteristics of meat products (Jeremiah & Gibson, 2003) as a result of functions of protein denaturation and compartmentalization of
uids in the protein matrix. However, in order to ensure microbial safety
of ready-to-eat meat products, a minimum core temperature of 73.9 C
has been recommended by USDA (USDA-FSIS, 2012). Boiling in water is
a high heat, wet thermal processing method associated with characteristic tastes, appearance and organoleptic properties. Heat penetrates
through food by convection from the surrounding liquid medium as a
result of the temperature gradient. Boiling in water causes the highest
cooking losses among meat cooking methods due to loss of water and
leaching of water soluble nutrients (Badiani et al., 2002). In order to ensure uniform cooking, the process should be slow. Protein denaturation,
along with complex changes in avor attributes, is the most desired
consequence of cooking and the physicochemical state of myobrillar

M.A. Khan et al. / Innovative Food Science and Emerging Technologies 21 (2014) 5057

proteins determines the quality of processed meat (C. T. Li & Wick,


2001).
High pressure processing (HPP) is an important emerging, sustainable technology which has the potential to be used in many areas of
food processing, including fruit and fruit juices, vegetables, meat and
seafood (Kruk et al., 2011), with minimal damage to product characteristics, thus making it a safe and consumer friendly food processing
method. In the meat sector, its application has continuously increased,
particularly for enhancing shelf life and safety of raw, and of sliced
cooked products. However, little attention has been directed towards
the development of ready-to-eat meat products with high pressure.
Changes observed in HPP-treated meats are largely associated with denaturation of proteins, however the mechanism is different from that of
heat processing. Pressure has been also shown to cause an increase in
solubilization of myosin and actin, together with some other proteins,
and produce increased interactions between myobrillar water and
proteins (A. L. Sikes, Tobin, & Tume, 2009). Processing under high pressure is associated with lower energy input (Smelt, 1998). Furthermore,
adiabatic compression has been reported to increase the temperature of
system by 23 C per 100 MPa (Jimnez Colmenero, 2002), depending
upon the type of pressure uid medium used, and the rate of pressure
increase. During application of pressure, and dependent upon the actual
pressure applied, muscle pH may decrease by 0.20.5 units due to the
decrease in volume of protein bound water (Cheftel & Culioli, 1997).
However, upon release of pressure, pH increases by about 0.2 units
above the initial pH of the raw meat due to loss of meat acid groups
caused by protein denaturation (A. Sikes, Tornberg, & Tume, 2010).
Breakdown in secondary, tertiary and quaternary structures brings
about modications in protein structures and functions (Campus, 2010).
So, achieving efcient denaturation of proteins in the myobrillar matrix,
by combining heat and pressure, will accelerate the cooking kinetics. HPP
alone has been reported to enhance the microbial safety of raw meat
(Simonin, Duranton, & de Lamballerie, 2012) and not adversely affect
the oxidative stability of dry-cured hams at lower pressures (Clariana,
Guerrero, Srraga, & Garcia-Regueiro, 2012). High pressure has been
used in combination with sodium chloride and phosphates to enhance
texture, water retention and color of pork meat (Villamonte, Simonin,
Duranton, Chret, & de Lamballerie, 2012) and beef batters (A. L. Sikes
et al., 2009). HPP improved the appearance and microbial safety of
smoked cod (Montiel, De Alba, Bravo, Gaya, & Medina, 2012). At higher
pressures (up to 800 MPa) there are reports of increased hardness of
beef post-rigor M. longissimus dorsi, even at temperatures below 60 C
(Ma & Ledward, 2004). Similarly, no improvement in tenderness was
observed for beef M. sternomandibularis until pressure-heat treated
muscle (200 MPa, 60 C, 20 min) was cooked (A. Sikes et al., 2010).
Salted duck meat of the Nanjing style, is very popular in many Asian
countries. The process involves salting and infusing with delicate herbal
avors followed by heating in water at low temperatures. The highest
quality attained, based on avor and texture, is achieved when cooked
at low temperatures for long time (Liu, Xu, & Zhou, 2007). To our knowledge, no studies have been conducted on salted duck meat treated with
high pressure. Similarly, there are no reports on the effects of simultaneous application of high pressure and high temperature on duck whole
muscles. HPP combined with a relatively low temperature (such as
70 C) for short processing duration (10 or 20 min) may contribute to
better texture and eating qualities of Nanjing style salted duck. The outcome of this research has signicant benets for meat processors and
consumers, in terms of enhanced product quality, as well as efciencies
in production.

51

weights 155165 g (13 1 4.0 0.5 1.5 0.5 cm3), were selected
for processing by a salting (3 h, 25 C), pickling (2 h, 25 C) according
to the method of Liu et al. (2007). Breasts were then brought to initial
temperatures either 10 or 40 C, and subsequently treated in a cooking
medium (Liu et al., 2007) as follows: Cooked control, heated at 95 C
(0.1 MPa) until the core temperature had reached 80 C; T1, pretreatment 10 C, then 70 C for 10 min; T2, pre-treatment 10 C,
then 70 C for 20 min; T3, pre-treatment 40 C, then 70 C for 10 min;
T4, pre-treatment 40 C, then 70 C for 20 min.
2.2. High pressure processing
An ultra-high pressure pilot plant (Model UHPF, 3.5 L capacity, capable of 8001000 MPa, Baotou Hi-tech Food Machinery Ltd., China) was
used for high pressure processing (HPP). The time to achieve 200 MPa
was 3min; therefore heating time of the 0.1MPa treatments was adjusted accordingly. The pressure chamber temperature was adjusted to
70 C with circulating water from a water bath. Up to three meat samples only were treated at a time in order to ensure uniform temperature
treatment. The temperature of the chamber was validated by a remote
sensing cell-type thermometer placed in an in-house designed aluminum alloy crucible which successfully withstood high pressure.
2.3. Cooking losses and product core temperature
After completion of treatments, the meat uids were drained and
the core temperature of the product was noted after 23 min air drying.
The cooking losses were calculated by the difference method and were
expressed as a percentage of initial weight. The nal product was immediately vacuum-sealed in pre-sterilized polyethylene bags and stored at
4 C for quality and microbial analysis.
2.4. Water compartmentalization and mobility
Proton NMR measurements were performed on lean meat samples
(~1.0 1.0 1.0 cm3) at room temperature 45 h after treatment on a
Niumag Pulsed NMR analyzer (PQ001, Niumag Corporation, Shanghai,
China) operating at a resonance frequency of 23MHz at 30C, essentially
as described by (Li et al., 2012). Transverse relaxation (T2) measurements were processed using the program MultiExp Invert Analysis 4.6
(Niumag Corporation, Shanghai, China) provided with the instrument.
2.5. Differential scanning calorimetry (DSC)
DSC measurements were performed on the lean meat samples
stored at 4 C during the period from 1 to 24 h after treatment. Samples
(~100mg) were tempered at 20C for 5min, and then heated from 20 to
120C at a scanning rate of 1C/min, with an empty ampoule as reference,
using a multi cell differential scanning calorimeter (TA Instruments,
Lindon, UT 84042, USA). The data were analyzed using the software
(Universal Analysis 2000, Version 4.5A, Build 4.5.0.5, TA Instruments,
Waters LLC) supplied with the machine.
2.6. Microbial evaluation
Aseptically vacuum-packed samples (5 g) stored overnight at 4 C
were comminuted and homogenized with 45mL (0.85% w/v) NaCl solution and incubated at 37 C for 72 h for determination of total aerobic
count on Plate Count Agar (PCA, Oxoid, UK) by serial dilutions method.
Colonies were expressed as log cfu/g.

2. Materials and methods


2.7. Optical properties
2.1. Optimization of processing conditions
Frozen Cherry Valley duck breasts were obtained from a duck processing plant in Shandong Province, China. Whole skin-on muscle of

Color measurements were performed within 23 h of processing


from upper, central and lower positions of core samples using a Minolta
colorimeter (L*a*b* scale coordinates) calibrated against a white tile.

M.A. Khan et al. / Innovative Food Science and Emerging Technologies 21 (2014) 5057

The values of chroma, hue, color distance and whiteness were derived
from L*a*b* coordinates to obtain further insight into meat color parameters according to the method of (Dai et al., 2013).
2.8. Textural analysis
The rheological measurements of the meat samples (~1 1 2.5 cm3)
were performed at room temperature within 23h of processing using an
aluminum cylindrical probe (SMP P/50, at bottom, diameter 50 mm)
using a texture prole analyzer (Model TA-XT 2i, Stable Micro Systems
Ltd., Godalming, England) essentially according to the procedure of
Angsupanich & Ledward (1998). Each sample was subjected to two
compressions 5 s apart with a pretest speed of 1.00 mm/s, test speed
5.00 mm/s, post-test speed 5.00 mm/s and trigger force of 0.005 kg. Numerical data was generated by software (version 4.0.12.0, stable Micro
systems Ltd., England) provided with the instrument.
2.9. Data analysis
The experimental observations were subjected to statistical analysis
using IBM SPSS Statistical Package 16.0 (SPSS Inc., Chicago, IL, USA). The
signicance of effect of treatments was determined by analysis of variance
(ANOVA). Means were compared for signicance (P b 0.05) by Duncan
multiple range test. The Principal component analysis was performed
using XLSTAT add-in (version 15.4.08.2633, Addinsoft, USA).
3. Results and discussion
3.1. Cooking losses and product core temperatures
The cooking losses, based on skin-on breast after brining, ranged
from 6 to 30%, depending upon the method of treatment (Fig. 1a). The
cooked control samples (cooked to a core temperature of 80 C) experienced the highest (P b 0.05) cooking losses (27.731.6%) among the
treated samples, while those samples heated at 0.1 MPa for 10 min, exhibited the lowest cooking losses (6.08.3%). Application of HPP at 70 C
yielded a cooked product having an intermediate cooking loss of about
8.314.5%. This represents a very large improvement in yield and presumably juiciness of the product. The higher cooking losses of salted
duck breast with HPP compared with heat-alone samples might be
attributed to the initial salting and pickling processes. Generally, the
cooking losses were independent of the initial pretreatment temperature (10 or 40 C), with exception of samples later processed at
200 MPa for 20 min. However, cooking losses were signicantly affected by duration of heating at 70 C or the time of pressure-heat

35

Cooked control
0.1 MPa
200 MPa

Cooking Losses (%)

30
25
20
15
10

de

de

application. Also, samples heated with, and without pressure treatment,


showed signicant differences for cooking losses (P b 0.05). Given that
pressure treatment generally results in an increase in temperature
(Fig. 1b) compared with heat alone, as a consequence of adiabatic
heating, the observed increases (P b 0.05) in cooking losses with pressure were as expected.
Fig. 1b shows the core temperatures of the duck breast following
various cooking and pressure-heat treatments. The nal temperatures
ranged from 53 to 80 C depending upon the method of treatment. As
expected, the cooked control samples had the highest temperatures.
Samples heated with or without pressure for 20min had higher temperatures (6164 C at 0.1 MPa, 6567 C at 200 MPa) than those heated for
10 min (5457 C at 0.1 MPa, 5360 C at 200 MPa). The samples exhibited signicant differences (P b 0.05) for all the pre-treatment temperature, pressure and duration of treatment; and increasing them increased
core temperatures signicantly (P b 0.05). USDA recommends a minimum core temperature of 73.9 C for the safe eating of ready-to-eat
poultry products (USDA-FSIS, 2012). When food systems are thermally
treated, certain temperature-dependent reactions proceed, which can
result in quality deterioration and nutrient loss related to thermal denaturation of meat proteins and redistribution of myobrillar water. The
net outcome of this is a loss of water and therefore a greater cooking
loss (Hanne Christine Bertram, Wu, van den Berg, & Andersen, 2006).
While a lower cooking temperature can improve yield and certain quality attributes, it can pose serious challenges for product safety. In the
work described here, the temperature of the products matched the temperature of the compression uid. The higher cooking losses (Pb0.05) of
the pressure treated samples at 70C, compared with those of heat-only
samples, implied that a combination of initial temperatures and pressure accelerated cooking kinetics as a result of adiabatic temperature
increase (Cheftel & Culioli, 1997). The lower cooking losses of the
pressure-heated samples compared with those cooked to 80 C imply
higher retention of water, which will result in improved texture and enhanced water holding capacity of meat because of pressure-induced denaturation of sarcoplasmic proteins (Marcos, Kerry, & Mullen, 2010)
that occurs at higher temperatures. Additionally, the reduction in cooking
losses is related to improvement of yield, which directly relates to greater
productivity and protability for the food processing industry. Furthermore, the reduced leaching would suggest an improvement in the nutritional qualities of the end product.
3.2. Water compartmentalization and mobility
The data related to proton spinspin relaxation times and their
corresponding proton populations are presented in Table 1. T2b and

Cooked control
0.1 MPa
200 MPa

100

Core temperatures (C)

52

90

80

70
60

e
h i

50
40

Cooked T1
control

T2

T3

T4

Cooked T1
control

T2

T3

T4

Fig. 1. Effect of pressure and heat treatment on cooking losses (a) and core temperatures (b) of duck breast samples. Samples were treated as follows: Cooked control, cooked to a core
temperature of 80 C; T1, pre-treatment 10 C, then 70 C for 10 min; T2, pre-treatment 10 C, then 70 C for 20 min; T3, pre-treatment 40 C, then 70 C for 10 min; T4, pre-treatment
40 C, then 70 C for 20 min. Values having different superscript letters are signicantly different, P b 0.05 (Duncan's multiple range test). Error bars are displayed for SD (n = 6).

M.A. Khan et al. / Innovative Food Science and Emerging Technologies 21 (2014) 5057

P2b represent relaxation times and proton populations related to


structurally-bound water. However, the fast- and slow-relaxation
times (T21 and T22, respectively), and their corresponding proton populations (P21 and P22, respectively), are considered to be the most important indices of water mobility and compartmentalization in
myobrillar systems (Pearce, Rosenvold, Andersen, & Hopkins, 2011).
The cooked control samples exhibited the lowest fast-relaxation times
(T21), followed by the samples heated for 20 min, with or without pressure treatment. The mean values of samples treated at 200 MPa
were slightly lower than those of heat-only samples. The proton
population representing immobilized water (P21), on the other
hand, exhibited three distinct compartments with signicantly
highest (P b 0.05) values for pressure treated samples, followed by
heat-only samples, and the lowest values for cooked control samples. Duration of heating also affected compartment sizes of fast
relaxing protons at 0.1 MPa, and samples processed for 20 min possessed smaller P21 compartment sizes than those of 10 min.
High pressure treated samples showed slightly lower slow-relaxation
times (T22) than optimum pressure treated samples. Duration of treatment signicantly affected T22, and the samples heated for 10 min exhibited the highest values. Cooked control, as well as pressure-treated
samples heated for 20 min had similar values for slow-relaxation times.
The proton population representing free water (P22) exhibited the most
drastic changes. Contrary to fast-relaxing proton populations, pressure
treated samples had the smallest P22 compartments. Signicant differences were observed resulting from the magnitude of pressure applied.
For non-pressurized treatments, signicant differences also existed for
heating times where longer heating times resulted in an increase in the
size of the P22 compartments without pressure. The cooked control samples, having been heated to a higher temperature (core temperature
80 C), had the largest P22 compartments. The mobility of protons in
the heated systems can be explained by the rate of reaction. The equilibrium position of water mobility is greatly affected by pressure. At 70 C,
there were no signicant differences among 0.1 and 200 MPa samples
for T21 and T22 values; however, increase in pressure shifted the equilibrium position of myowater from inter-myobrillar spaces towards myobrils. Of particular note, the heating times, or initial temperature, did not
appear to affect relaxation times or populations associated with slow
relaxing protons signicantly. The decrease in the values of T21 and increase in T22 (Table 1) during initial cooking stages are likely to be related
to denaturation of myosin (Bertram et al., 2001), which causes contraction of myobrils and results in expulsion of water from myobrils to
the inter-myobrillar spaces. Although, water exists in the myobrillar

53

matrix as free, immobilized and protein associated, continuous exchange


continues between these compartments (Bertram & Andersen, 2004).
High temperature is responsible for outward movement of released protons due to denaturation of proteins, while in a pressurized system, the
released protons do not follow an outward expulsion. For this reason,
the pressure affected systems resulted in a smaller free water compartment, and a larger immobilized water compartment. Also, the pressureassociated denaturation of proteins followed an entirely different mechanism. Proteins obey the Le ChatelierBraun principle under pressure, and
so reduction in volume of the system affects their structure due to partial
unfolding of proteins (Pereira & Vicente, 2010).
3.3. Differential scan calorimetry (DSC)
Three endothermic transitions were observed with increasing
temperatures in raw, salted and pickled samples, representing myosin (peak denaturing temperature 55 5 C), then a combination of
connective tissue proteins and sarcoplasmic proteins (65 5 C)
and nally actin (75 5 C). However there were signicant reductions
in peak areas resulting from denaturation of the rst and third peaks in
salted and pickled samples (Fig. 2a). There was a shift in peaks to higher
temperatures of endothermic transitions under all processing conditions, which indicated decreases in the enthalpies of protein denaturation. Heating generally causes protein denaturation (FernndezMartn, Fernndez, Carballo, & Colmenero, 1997), as the rst and second
peaks of heat-only samples completely vanished at 10 and 20 min
(Fig. 2a). However, a broad peak with a transition temperature near
80C remained more or less unchanged, irrespective of treatment duration. The DSC curve of the cooked control sample showed essentially the
complete absence of peaks except for that near 80 C. High pressure
treated samples (Fig. 2b) also resulted in the complete loss of the myosin peak. As previously observed (A. Sikes et al., 2010), high pressure
preserved the second endothermic transitions, although smaller peak
areas suggested more protein denaturation at higher processing times.
This supports the observations that connective tissue components such
as collagen are stabilized by pressure treatment. Actin was the most adversely affected by high pressure, as this third peak exhibited the least endothermic transitions at all the processing durations. Differences in the
initial holding temperatures did not bring about any signicant differences in protein denaturation.
Under simultaneous pressure and heat treatments, protein denaturation occurs by the two mechanisms, as they each induce an interdependent antagonistic-like effect on the protein matrix (Fernndez

Table 1
Water mobility and relative size of compartments of whole skin-on duck breast following treatments as determined by NMR spectroscopy.1
Relaxation times (ms)2

Cooked control
(Cooked to a core temperature of 80 C)
0.1 MPa
Pre-treatment 10 C, then
70 C for 10 min
70 C for 20 min
Pre-treatment 40 C, then
70 C for 10 min
70 C for 20 min
200 MPa
Pre-treatment 10 C, then
70 C for 10 min
70 C for 20 min
Pre-treatment 40 C, then
70 C for 10 min
70 C for 20 min
1

Relative compartment sizes3

T2b

T21

T22

P2b

P21

P22

7.13 1.02a

40.47 3.09c

152.98 19.05c

5.01 1.34a

82.19 2.43c

12.82 2.63a

7.15 1.2a
7.61 0.84a

47.61 3.35ab
46.53 3.56ab

196.61 10.59a
188.41 20.69ab

3.86 0.69bcd
4.17 0.99abc

91.07 2.22b
84.18 1.4c

5.09 2.38b
11.66 1.52a

7.28 0.98a
7.59 0.58a

49.78 0.01a
45.45 3.35b

192.2 13.52a
155.79 9.3c

3.57 0.46cd
4.84 0.74ab

91.48 2.19b
83.2 1.52c

4.96 1.96b
11.97 1.65a

4.48 2.03b
4.27 1.63b

47.61 3.35ab
45.45 3.35b

170.96 9.3bc
160.66 23.93c

2.09 0.65e
2.1 0.7e

94.72 2.19a
95.53 0.94a

3.21 2.5bc
2.38 0.91c

5.31 1.12b
5.34 1.75b

47.61 3.35ab
44.37 2.65bc

163.38 12.47c
152.5 13.63c

2.04 0.97e
2.93 0.25de

95.68 0.33a
95.47 0.43a

2.3 1.25c
1.61 0.58c

Values are means SD, n = 6. Values in columns having different superscript letters are signicantly different, P b 0.05 (Duncan's multiple range test).
Peak relaxation times associated with structurally bound water, T2b; immobilized water, T21; free capillary water, T22.
3
Relative compartment sizes based on areas of proton populations of structurally bound water, P2b; immobilized water, P21; free capillary water, P22.
2

54

M.A. Khan et al. / Innovative Food Science and Emerging Technologies 21 (2014) 5057

Fig. 2. DSC thermogram showing the extent of protein denaturation of duck skin-on whole breast muscle as a function of initial temperature, heating time and pressure. Samples were
treated as follows: Fresh, raw meat; Salted, rubbed with salt mixture at room temperature for 3 h; Pickled, dipped in brine solution at room temperature for 2 h; Control, cooked to a
core temperature of 80 C; T1, pre-treatment 10 C, then 70 C for 10 min; T2, pre-treatment 10 C, then 70 C for 20 min; T3, pre-treatment 40 C, then 70 C for 10 min; T4, pretreatment 40 C, then 70 C for 20 min.

numbers (P b 0.05). The microbial load of cooked control samples


was signicantly lower than all the samples treated at 0.1 MPa. Heat destroys microorganisms by denaturing proteins and disrupting membrane
functions. In the present study, moist heat, heating temperatures and
application times played critical roles for destruction of bacteria. As previously observed (Pelczar, Chan, & Kreig, 1993), moist heat caused coagulation and denaturation of essential proteins at 60 to 70 C for 5 to 10 min,
which killed vegetative cells of bacteria due to disrupting membrane
functions. Heat application at 70C for 10 and 20min reduced the number
of microbes, however any spores present would not be eliminated, and so
might germinate at a later time thus giving high microbial numbers. According to Food Safety Australia New Zealand, the standard total aerobic
plate count for ready-to-eat products not intended for further slicing
should be b104 (cfu/g) (FSANZ, 2001), so the heat-only samples, with
the exception of the cooked control, were not safe for consumption.
Pressure-heat treatments exhibited the lowest microbial numbers as
their log cfu/g values were signicantly lower (P b 0.05) than those of
heat-alone, as well as for the cooked control samples. However, there
were no signicant differences with time of heating, as well as pretreatment temperatures prior to application of high pressure. In earlier reports,
high pressures from 200 to 300MPa have been considered adequate to inactivate vegetative cells of molds and yeast at ambient temperature
(Smelt, 1998), while there was complete eradication of microbial contamination in meat subjected to 520 MPa for 1 h at 52 C after storage for

Microbial load (log cfu/g)

Martn, Otero, Solas, & Sanz, 2000). Myosin was completely denatured
by heating, with and without pressure, irrespective of treatment duration, as increase in surface hydrophobicity has been shown to denature
myosin under heating-alone and high-pressure (Cao, Xia, Zhou, & Xu,
2012). The second thermal transition represents sarcoplasmic and connective tissue proteins. Sarcoplasmic proteins began denaturation at
4060C, as they also did under high-pressure. However, since a portion
of the combined peak was retained after high pressure at 200 MPa and
70 C, it would appear that connective tissue has been stabilized as
reported previously (Fernandez-Martin, 2007). Collagen remains considerably stabilized by pressurization because of hydrogen bonding
within the triple -helical structure (FernndezMartn et al., 2000).
Furthermore, the area under second endothermic transition peak of
pressure-heated samples was considerably greater than those of cooked
control and heated-alone samples. Retention of connective tissue proteins (and possibly sarcoplasmic proteins) in case of high pressure treated samples could be explained by the rate equation. The rate constants
of these proteins possibly shifted their positions towards equilibrium
due to volumetric decrease under high pressure, which prevented their
further denaturation in their thermally active zones. Enzymes are generally unstable at high pressures (Angsupanich & Ledward, 1998), and
therefore the preservation of some of the muscle proteins could be due
to the absence of those enzymes in pressure-heat samples. In the present
study, actin remained the most labile moiety to heating with and without
pressure. Moreover, cooked control samples exhibited greater actin denaturation than heat-alone and pressure-heated samples. It is considerably
more thermo-stable, but quite sensitive to high pressure (Lee, Kim, Lee,
Hong, & Yamamoto, 2007). The samples treated under atmospheric pressures retained some actin residues because their denaturation temperatures were not fully achieved, while pressure-heated samples generally
underwent severe protein denaturation, possibly because of the higher
temperatures resulting from adiabatic heating. Overall, the rheology of
the pressure-heated samples improved due to greater degree of protein
denaturation, hence ensured more palatability than the cooked control,
as well as than heat-only samples.

7
5

4
3
2

The highest values (6.13 0.1 log cfu/g) of bacterial numbers were
observed for fresh, raw samples (Fig. 3). Various pretreatment temperatures did not have any signicant inuence on numbers. However,
heating-alone for 10 or 20min resulted in signicant reductions as compared to those of fresh samples. Under atmospheric pressure, longer
heat application times (20 vs. 10 min) resulted in lower microbial

d
e

0
Fresh Cooked
control

3.4. Microbial inactivation

Cooked control
0.1 MPa
Fresh
200 MPa

T1

T2

T3

T4

Fig. 3. Aerobic plate count (log cfu/g meat) of duck skin-on whole breast muscle as a function of initial temperature, heating time and pressure. Samples were treated as follows:
Cooked control, cooked to a core temperature of 80 C; T1, pre-treatment 10 C, then
70 C for 10 min; T2, pre-treatment 10 C, then 70 C for 20 min; T3, pre-treatment
40 C, then 70 C for 10 min; T4, pre-treatment 40 C, then 70 C for 20 min. Values having
different superscript letters are signicantly different, P b 0.05 (Duncan's multiple range
test). Error bars are displayed for SD (n = 6). Values having different superscript letters
are signicantly different, P b 0.05 (Duncan's multiple range test). Error bars are displayed
for SD (n = 6).

M.A. Khan et al. / Innovative Food Science and Emerging Technologies 21 (2014) 5057

3 weeks (Farr, 1990). High pressure (200 MPa) treatment at 70 C for 10


and 20 min caused greater reduction in microbial populations than
heat-alone samples because of pressure-induced denaturation of proteins (San Martin, Barbosa-Cnovas, & Swanson, 2002), lack of ATP synthesis and hydrolysis due to denaturation of enzymes (Farr, 1990),
interruption of cellular functions by decreasing the synthesis of ribosomes (Lado & Yousef, 2002), and disturbance of their membrane functions (uptake of nutrients and disposal of wastes) (Pagn & Mackey,
2000). The complete destruction of bacterial spores by high pressure
is achieved through initiation of germination, and then germinated
spores are susceptible to all the treatments (Paidhungat et al., 2002).
In the present study, the absence of microbial counts in duck breasts
conrmed that the combination of 200 MPa and 70 C for 10 or 20 min
was sufcient to eradicate bacterial vegetative cells and suggests that
these treatments are sufcient to produce microbiologically safe duck
breast products.
3.5. Meat color
The effect of treatments on color of duck breast is presented in
Table 2. Cooked control samples exhibited the highest values for lightness (L*), yellowness (b*), hue angle (h), color distance (E) and whiteness (W), but the lowest values for redness (a*) and chroma (C*). The
lower redness of cooked control samples was attributed to extended exposure to the high temperature medium. Heat-alone samples treated
for 10 min exhibited the lowest values for L*, b*, h, E and W whereas
treatment for 20 min signicantly increased their values, but decreased
values for a* and C*. The increases in L*, b*, h, E and W with thermal
processing suggest increased precipitation of myobrillar and sarcoplasmic proteins (Dai et al., 2013), whereas decreases in a took place
due to increased denaturation of myoglobin (Cheah & Ledward, 1997).
The samples subjected to pressure-heat exhibited higher values for L*,
E and W compared with the heat-only samples at the respective processing times. The lighter appearance of meat and increase in W of
salted duck samples at 200 MPa compared with heat-only samples can
be considered as indicative of greater protein denaturation (Tseo,
Deng, Cornell, Khuri, & Schmidt, 2006). Pressure, as well as treatment
duration, did not cause any signicant effects on a* values (P N 0.05).
Pressure-heated samples did not show signicant differences for b*, C*
and h compared with heat-only samples for any of the processing
times. The initial temperatures only affected L*, E and W values signicantly with pressure and heating times. High pressure accelerated the
changes occurring in the protein matrix of the meat system, so the pressure treated samples achieved similar lightness as that of cooked control
at signicantly lower times and temperatures. The optical parameters of

55

HPP samples treated for 10 min were statistically similar (P N 0.05) to


those treated without HPP for 20 min, while HPP samples treated for
20 min exhibited similar (P N 0.05) results to those of cooked control.
The color improvement of the pressure-heated samples took place because of denaturation of metmyoglobin and partly due to the rupture
of hydrophobic interactions (Cheah & Ledward, 1997). The increase in
L* values in the current study are in agreement with an earlier study
on minced beef, packed under vacuum, air or oxygen, and subjected to
200350 MPa at 10C for 10 min. We were unable to observe any significant effect of treatment on a* values of salted duck meat which differs
from the above authors, who observed a decrease in a* values at 400
500 MPa. Increasing treatment duration under optimum pressure increased h (dominant wavelength) values; its increase was related to
denaturation of myoglobin or displacement of heme molecule in earlier
reports (Ramirez-Suarez & Morrissey, 2006). On the other hand, increasing pressure and heating times decreased C* (color depth) values. HPP has
been associated with reduced yellowness (Ferrini, Comaposada, Arnau, &
Gou, 2012). However, in the present studies, pressure-heat treatment did
not show signicant differences in yellowness. The strong correlations observed between different optical parameters suggested that the variations
in L*, a* and b* all contributed to the total color changes.
3.6. Textural analysis
All three samples (cooked controls, heat only and pressure-heat
treated) were well separated from each other based on hardness measurements (Table 3). Cooked control samples exhibited the highest
values of hardness, springiness, cohesiveness, resilience, gumminess and
chewiness, while adhesiveness was only greater than those of heat-only
samples treated for 20 min. At ambient pressure, increasing time of
heating increased attributes of hardness, springiness, gumminess and
chewiness, but decreased adhesiveness and resilience. Initial pretreatment temperature (10 or 40 C) did not affect the heat-only samples for
any of the textural measurements. In the heat-only samples, collagen
was expected to begin denaturation at 6065 C, however, the temperature rose to 70 and 80C in heat-only and cooked control samples, respectively, resulting in shrinkage of myobrillar structures which contributed
to increased hardness. Increase in springiness in the non-pressure treated
samples agrees with earlier reports for beef muscles heated from 60 to
70 C (Palka & Daun, 1999). The cohesiveness results of the heat-only
samples were signicantly lower than those of the cooked control,
which differ from earlier reports (Yuste, Mor-Mur, Capellas, Guamis, &
Pla, 1999).
The pressure-heat samples behaved differently, as they exhibited
the least values for hardness, cohesiveness, gumminess and chewiness.

Table 2
Optical properties of whole skin-on duck breast core following treatments as measured by Minolta colorimeter.1

Cooked control
(Cooked to a core temperature of 80 C)
0.1 MPa
Pre-treatment 10 C, then
70 C for 10 min
70 C for 20 min
Pre-treatment 40 C, then
70 C for 10 min
70 C for 20 min
200 MPa
Pre-treatment 10 C, then
70 C for 10 min
70 C for 20 min
Pre-treatment 40 C, then
70 C for 10 min
70 C for 20 min
1

Lightness

Redness

58.14 0.6a

13.42 3.05c

Yellowness
9.6 1.01a

Chroma

Hue

Color distance

Whiteness

16.65 2.06d

0.64 0.15a

60.51 0.6a

54.93 1.17a

51.58 0.62d
55.29 0.73b

19 1.03a
18.04 0.66ab

8.04 0.77cd
9.15 0.64ab

20.64 1.16ab
20.24 0.56abc

0.41 0.03cd
0.48 0.04bc

55.57 0.67d
58.88 0.66b

47.36 0.78f
50.93 0.75c

53.1 0.73c
55.29 0.74b

19.47 1.69a
16.87 0.96b

7.91 0.55d
9.05 0.87abc

21.04 1.44a
19.16 1.07bc

0.4 0.05d
0.5 0.04b

57.13 0.98c
58.53 0.85b

48.59 0.73e
51.36 0.71c

53.52 0.65c
57.85 0.66a

17.76 1.04ab
16.6 1.06b

7.76 0.96d
8.36 0.63bcd

19.41 0.97bc
18.6 1.02c

0.42 0.06cd
0.47 0.04bcd

56.94 0.78c
60.78 0.76a

49.63 0.59de
53.93 0.64b

54.9 0.59b
58.26 0.91a

17.96 1.58ab
16.7 0.57b

8.66 0.71abcd
9.07 0.66ab

19.96 1.59abc
19.01 0.66bc

0.46 0.04bcd
0.51 0.03b

58.44 0.77b
61.29 0.85a

50.67 0.87cd
54.14 0.92ab

Values are means SD, n = 6. Values in columns having different superscript letters are signicantly different, P b 0.05 (Duncan's multiple range test).

56

M.A. Khan et al. / Innovative Food Science and Emerging Technologies 21 (2014) 5057

Table 3
Texture prole analysis of whole skin-on duck breast following pressure-heat treatmentst.1

Cooked control
(Cooked to a core temperature of 80 C)
0.1 MPa
Pre-treatment 10 C, then
70 C for 10 min
70 C for 20 min
Pre-treatment 40 C, then
70 C for 10 min
70 C for 20 min
200 MPa
Pre-treatment 10 C, then
70 C for 10 min
70 C for 20 min
Pre-treatment 40 C, then
70 C for 10 min
70 C for 20 min

Hardness
N

Springiness
-

Adhesiveness
gs

Cohesiveness

Resilience

Gumminess

Chewiness

75.89 1.72a

0.67 0.02a

26.68 3.78d

0.67 0.02a

0.34 0.03a

50.84 0.98a

33.92 0.87a

53.59 0.92c
59.21 0.22b

0.62 0.01de
0.64 0.01bc

22.01 3.7bc
31.07 4.61e

0.63 0.05bc
0.65 0.01ab

0.33 0.02a
0.31 0.01b

33.38 2.22c
38.23 0.54b

20.55 1.19d
24.35 0.49b

52.65 1.02c
58.72 1.28b

0.62 0.01e
0.64 0.01bc

0.62 0.04c
0.63 0.02bc

0.33 0.03a
0.31 0.01b

32.17 1.91c
36.96 0.92b

19.72 1.05d
23.49 0.71c

33.7 0.64d
30.1 1.16e

0.63 0.03cde
0.65 0.01b

12.45 1.91a
19.93 1.75b

0.61 0.02cd
0.58 0.01de

0.34 0.02a
0.29 0.01c

20.37 0.67d
17.35 0.7e

12.72 0.16e
11.23 0.47f

33.47 0.79d
30.21 0.61e

0.63 0.02cd
0.65 0.01b

13.49 1.72a
23.74 2.32bcd

0.61 0.02cd
0.56 0.02e

0.33 0.01a
0.28 0.01c

20.14 0.65d
16.89 0.77e

12.65 0.54e
10.88 0f

24.6 4.19cd
36 3.64f

Values are means SD, n = 6. Values in columns having different superscript letters are signicantly different, P b 0.05 (Duncan's multiple range test).

Increasing time of pressure-heat treatment further decreased hardness,


resilience, gumminess and chewiness. The effect of high pressure was so
pronounced that the hardness of samples pressure-heat treated for
10 min was lower than those treated for 20 min. The lower hardness
values of the pressure treated samples could not be attributed to
lower core temperatures alone, as they were also signicantly lower
than the hardness values of non-pressure treated samples. The samples
followed a similar trend for gumminess. Our results are in agreement
with Ma and Ledward (2004) for beef, in which they found higher tenderness for samples heated under high pressure and heat than with
heat- or high pressure-alone. The low cohesiveness values of pressureheated samples in the current study are also in agreement with earlier
reports (Ma & Ledward, 2004), who reported a decrease in cohesiveness
at 70 C with application of pressures from 200 to 800 MPa. On the contrary, an increase in springiness with increasing time under HPP showed
an increase in the elastic character of meat which has been related to
unfolding of actin (Angsupanich & Ledward, 1998). Adhesiveness increased with time irrespective of nature of treatment, and differs
from the ndings of Angsupanich and Ledward (1998). Decrease in
hardness, adhesiveness and chewiness under heat and pressure indicate increased denaturation of myosin and collagen (Angsupanich &
Ledward, 1998), which is in agreement with our DSC results. Taking
all attributes into consideration, this indicates that, compared with
the non-pressure treated samples, the pressurized samples required
less chewing for bringing the bolus to a suitable state for swallowing,
and improved tenderness. Similarly, the ndings suggest that cooked
control samples required more effort for disruption than did the
pressure-heated samples. The difference in behavior was attributed
differences in exposure time to the pressure and heating medium.

within myobrillar systems. The aggregation of actomyosin under high


pressure leads to the formation of crosslinks, and increases the unfolding
of proteins into myobrillar protein network (Egelandsdal, Fretheim, &
Samejima, 1986), which causes the contraction of myobrils and results
in expulsion of water from myobrils to the inter-myobrillar spaces.
The slow-relaxation proton compartments were negatively affected by
the denaturation enthalpies of proteins, suggesting protein denaturation
is the cause of the loss of free myobrillar water. The changes in the
sizes of fast-relaxation proton compartments were strongly correlated
with the changes occurring in the denaturation enthalpies of sarcoplasmic
and connective tissue proteins. High pressure treatment strengthens
hydrogen bonds of the protein matrix in the muscle systems (Sun &
Holley, 2010). In the current study, the increase in denaturation enthalpies of sarcoplasmic and connective tissue was attributed to the
strengthening of hydrogen bonds within the triple -helical structure
of collagen (FernndezMartn et al., 2000). The similarity of water
and collagen in terms of hydrogen bonding in their structures explains
the presence of fast-relaxation compartment and denaturation enthalpies of sarcoplasmic and connective tissue being in the same

5
Denaturation
enthalpy of
actin

3
Slow-relaxation
times

Slow-relaxation
proton
compartment

Total enthalpy
Fast-rexation of denaturation
times

The principal component analysis of denaturation enthalpies of sarcoplasmic and connective tissue proteins and mobility and compartment sizes of fast- and slow-relaxation protons in duck meat samples
subjected to high pressure and heat treatments is presented in Fig. 4.
The rst two principal components explained 80.28% of the total variation occurring in the duck meat samples under heating and pressurization condition. The results revealed that a relationship existed between
denaturation enthalpies of protein and T2 relaxation values of protons
in the myobrillar matrix and the modications in the protein structures regulating the sizes of proton compartments. The placement of
fast and slow T2 relaxation times in the rst quadrant with denaturation
enthalpies of actin and total enthalpy of denaturation suggested the existence of relationships between these proteins on the mobility of water

F2 (34.76 %)

3.7. Principal component analysis

-5

-3

-1

1
-1

-3

5
Fast-relaxation
proton
compartment

Denaturation
enthalpies of
Sarcoplasmic
and connective
tissue proteins

-5
F1 (45.52 %)

Fig. 4. Relationship between denaturation enthalpies of proteins and mobility and compartment sizes of fast- and slow-relaxation protons in duck meat samples subjected to
high pressure and heat treatments.

M.A. Khan et al. / Innovative Food Science and Emerging Technologies 21 (2014) 5057

quadrant of principal component analysis. High pressure-heat treatment in this study affected the protein contents of the duck meat
samples, which ultimately contributed to the changes in water mobility and compartmentalization within the myobrillar system.
4. Conclusions
This study involved the simultaneous application of high pressure
(200 MPa) and heat (70 C) to produce a ready-to-eat Nanjing-style
salted duck meat product. The pressure-heated samples exhibited greater
cooking losses than heat-alone samples at treatment times of 10 and
20 min, but smaller losses than those of cooked control. High pressure
treatment at 70 C was responsible for the greater water retention in
the fast-relaxation compartment. Higher degree of denaturation of myobrillar proteins ensured improved rheological character and palatability
of pressure-heated samples. The observation that some sarcoplasmic and
connective tissue proteins remained after pressure-heat treatment, but
not with heat-alone, suggested that denaturation of proteins occurred
by different mechanisms under high pressure and heat. This was further
supported by the greater denaturation of actin with pressure-heat than
with heat-alone. Furthermore, application of high pressure and heat resulted in improved tenderness and microbial safety at both treatment
times compared with the heat-only and cooked control samples. The optical properties of pressure-heated samples at reduced temperatures and
times were comparable to those of the cooked control. The results indicated that pressure-heat treatment used in the present study ensured
enhanced yield, palatability and microbial safety and was suitable for
preparation of a ready-to-eat Nanjing style salted duck product. Followup studies will be conducted to investigate the avor and oxidative
shelf-stability of pressure-heat treated products.
Acknowledgments
The authors are highly indebted to Ministry of Education, P.R. China
(200903012), Ministry of Agriculture, P.R. China (NCET-11-0668) and
The Islamia University of Bahawalpur, Govt. of Pakistan, for providing nancial support for this study.
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