Professional Documents
Culture Documents
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
M.A. Khan et al. / Innovative Food Science and Emerging Technologies 21 (2014) 5057
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.
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
30
25
20
15
10
de
de
Cooked control
0.1 MPa
200 MPa
100
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
53
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
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.
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
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
55
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).
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 %)
-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.
References
Angsupanich, K., & Ledward, D. (1998). High pressure treatment effects on cod (Gadus
morhua) muscle. Food Chemistry, 63(1), 3950.
Badiani, A., Stipa, S., Bitossi, F., Gatta, P. P., Vignola, G., & Chizzolini, R. (2002). Lipid composition, retention and oxidation in fresh and completely trimmed beef muscles as
affected by common culinary practices. Meat Science, 60(2), 169186.
Bertram, H. C., & Andersen, H. J. (2004). Applications of NMR in meat science. Annual
Reports on NMR Spectroscopy, 53, 157202.
Bertram, H. C., Karlsson, A. H., Rasmussen, M., Pedersen, O. D., Donstrup, S., & Andersen, H.
J. (2001). Origin of multiexponential T2 relaxation in muscle myowater. Journal of
Agricultural and Food Chemistry, 49(6), 30923100.
Bertram, H. C., Wu, Z., van den Berg, F., & Andersen, H. J. (2006). NMR relaxometry and
differential scanning calorimetry during meat cooking. Meat Science, 74(4), 684689.
Campus, M. (2010). High pressure processing of meat, meat products and seafood. Food
Engineering Reviews, 2(4), 256273.
Cao, Y., Xia, T., Zhou, G., & Xu, X. (2012). The mechanism of high pressure-induced gels of
rabbit myosin. Innovative Food Science & Emerging Technologies, 16, 4146.
Cheah, P., & Ledward, D. (1997). Inhibition of metmyoglobin formation in fresh beef by
pressure treatment. Meat Science, 45(3), 411418.
Cheftel, J. C., & Culioli, J. (1997). Effects of high pressure on meat: A review. Meat Science,
46(3), 211236.
Clariana, M., Guerrero, L., Srraga, C., & Garcia-Regueiro, J. A. (2012). Effects of high
pressure application (400 and 900 MPa) and refrigerated storage time on the oxidative stability of sliced skin vacuum packed dry-cured ham. Meat Science, 90(2),
323329.
Dai, Y., Miao, J., Yuan, S. -Z., Liu, Y., Li, X. -M., & Dai, R. -T. (2013). Colour and sarcoplasmic
protein evaluation of pork following water bath and ohmic cooking. Meat Science,
93(4), 898905.
Egelandsdal, B., Fretheim, K., & Samejima, K. (1986). Dynamic rheological measurements
on heat-induced myosin gels: Effect of ionic strength, protein concentration and addition of adenosine triphosphate or pyrophosphate. Journal of the Science of Food and
Agriculture, 37(9), 915926.
Farr, D. (1990). High pressure technology in the food industry. Trends in Food Science and
Technology, 1, 1416.
57