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 a b s t r a c t

Article history: This study investigated the effects of high pressure, in combination with heat, for development of a ready-to-eat
Received 3 June 2013 salted duck meat product. Duck breast was subjected to a salting and pickling process prior to either heating-
Accepted 19 October 2013 alone (70C) or high-pressure (200MPa) with heating (70C) for 10 or 20min, and compared with a cooked con-
trol (core temperature 80C at 0.1MPa) for quality assessment. Compared with the cooked control, pressure-heat
Editor Proof Receive Date 15 November 2013
treated samples exhibited reduced cooking losses, and NMR showed they had larger fast-relaxation proton com-
Keywords:
partments. Pressure-heat preserved some sarcoplasmic and connective tissue proteins, but caused greater dena-
High pressure processing turation of actin than with heat-only samples. The reduction in microbial load with pressure-heat indicated
Cooking suitability of the process for ready-to-eat products. Pressure-heat treatment did not affect color, but there was
Duck meat a decrease in hardness and gumminess, suggesting higher palatability. The reduction in cooking losses, resulting
Protein denaturation from altered proton compartmentalization, and changes in myobrillar proteins enhanced product acceptability.
NMR proton relaxation 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 mo-
bility by NMR, extent of protein denaturation by DSC, microbial numbers, surface color and texture which de-
scribed 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).
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 palat-
ability characteristics of meat products (Jeremiah & Gibson, 2003) as a re-
sult 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 character-
istic 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 en-
sure 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

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
proteins determines the quality of processed meat (C. T. Li & Wick,
2001).
High pressure processing (HPP) is an important emerging, sustain-
able 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 character-
istics, 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 de-
naturation 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 pres-
sure 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 knowl-
edge, no studies have been conducted on salted duck meat treated with
high pressure. Similarly, there are no reports on the effects of simulta-
neous 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 out-
come of this research has signicant benets for meat processors and
consumers, in terms of enhanced product quality, as well as efciencies
in production.
2. Materials and methods
2.1. Optimization of processing conditions
Frozen Cherry Valley duck breasts were obtained from a duck pro-
cessing plant in Shandong Province, China. Whole skin-on muscle of
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, 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.
2.2. High pressure processing
An ultra-high pressure pilot plant (Model UHPF, 3.5 L capacity, capa-
ble 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 adjust-
ed accordingly. The pressure chamber temperature was adjusted to
70 C with circulating water from a water bath. Up to three meat sam-
ples 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 alumi-
num 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 imme-
diately 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) measure-
ments 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 solu-
tion 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.
2.7. Optical properties
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.
52 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 param-
eters 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. Nu-
merical 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) expe-
rienced 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, ex-
hibited 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 pre-
sumably 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 temper-
ature (10 or 40 C), with exception of samples later processed at
200 MPa for 20 min. However, cooking losses were signicantly af-
fected by duration of heating at 70 C or the time of pressure-heat
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 pres-
sure 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 temper-
atures (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 exhib-
ited signicant differences (P b 0.05) for all the pre-treatment tempera-
ture, pressure and duration of treatment; and increasing them increased
core temperatures signicantly (P b 0.05). USDA recommends a mini-
mum 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 dena-
turation 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 qual-
ity attributes, it can pose serious challenges for product safety. In the
work described here, the temperature of the products matched the tem-
perature 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 pres-
sure 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 en-
hanced water holding capacity of meat because of pressure-induced de-
naturation 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. Further-
more, the reduced leaching would suggest an improvement in the nutri-
tional 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

a b
35 a Cooked control 100
Cooked control
0.1 MPa 0.1 MPa
30 200 MPa 90 200 MPa
Core temperatures (C)

a
Cooking Losses (%)

25
80
20
b c
b 70 d
15 c e f
e de de d
f 60 h i g
10 f
5 50

0 40
Cooked T1 T2 T3 T4 Cooked T1 T2 T3 T4
control control

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

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 pop-
ulations (P21 and P22, respectively), are considered to be the most im-
portant 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 pres-
sure 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 sam-
ples. Duration of heating also affected compartment sizes of fast
relaxing protons at 0.1 MPa, and samples processed for 20 min pos-
sessed 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 treat-
ment signicantly affected T22, and the samples heated for 10 min ex-
hibited 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 differ-
ences 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 sam-
ples, 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 equilib-
rium 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 equilib-
rium position of myowater from inter-myobrillar spaces towards myo-
brils. 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 in-
crease in T22 (Table 1) during initial cooking stages are likely to be related
to denaturation of myosin (Bertram et al., 2001), which causes contrac-
tion of myobrils and results in expulsion of water from myobrils to
the inter-myobrillar spaces. Although, water exists in the myobrillar
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 pro-
tons 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 compart-
ment, and a larger immobilized water compartment. Also, the pressure-
associated denaturation of proteins followed an entirely different mecha-
nism. 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 myo-
sin (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 condi-
tions, which indicated decreases in the enthalpies of protein dena-
turation. Heating generally causes protein denaturation (Fernndez-
Martn, 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 dura-
tion. 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 myo-
sin 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 ad-
versely affected by high pressure, as this third peak exhibited the least en-
dothermic transitions at all the processing durations. Differences in the
initial holding temperatures did not bring about any signicant differ-
ences in protein denaturation.
Under simultaneous pressure and heat treatments, protein denatur-
ation occurs by the two mechanisms, as they each induce an interde-
pendent 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 Relative compartment sizes3

T2b T21 T22 P2b P21 P22

Cooked control 7.13 1.02a 40.47 3.09c 152.98 19.05c 5.01 1.34a 82.19 2.43c 12.82 2.63a
(Cooked to a core temperature of 80 C)

0.1 MPa
Pre-treatment 10 C, then
70 C for 10 min 7.15 1.2a 47.61 3.35ab 196.61 10.59a 3.86 0.69bcd 91.07 2.22b 5.09 2.38b
70 C for 20 min 7.61 0.84a 46.53 3.56ab 188.41 20.69ab 4.17 0.99abc 84.18 1.4c 11.66 1.52a
Pre-treatment 40 C, then
70 C for 10 min 7.28 0.98a 49.78 0.01a 192.2 13.52a 3.57 0.46cd 91.48 2.19b 4.96 1.96b
70 C for 20 min 7.59 0.58a 45.45 3.35b 155.79 9.3c 4.84 0.74ab 83.2 1.52c 11.97 1.65a

200 MPa
Pre-treatment 10 C, then
70 C for 10 min 4.48 2.03b 47.61 3.35ab 170.96 9.3bc 2.09 0.65e 94.72 2.19a 3.21 2.5bc
70 C for 20 min 4.27 1.63b 45.45 3.35b 160.66 23.93c 2.1 0.7e 95.53 0.94a 2.38 0.91c
Pre-treatment 40 C, then
70 C for 10 min 5.31 1.12b 47.61 3.35ab 163.38 12.47c 2.04 0.97e 95.68 0.33a 2.3 1.25c
70 C for 20 min 5.34 1.75b 44.37 2.65bc 152.5 13.63c 2.93 0.25de 95.47 0.43a 1.61 0.58c
1
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).
2
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.
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, pre-
treatment 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 dura-
tion, 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 con-
nective 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 con-
siderably 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 pro-
teins (and possibly sarcoplasmic proteins) in case of high pressure treat-
ed 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 gener-
ally 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 dena-
turation 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 pres-
sures retained some actin residues because their denaturation tempera-
tures 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.
3.4. Microbial inactivation
The highest values (6.13 0.1 log cfu/g) of bacterial numbers were
observed for fresh, raw samples (Fig. 3). Various pretreatment temper-
atures did not have any signicant inuence on numbers. However,
heating-alone for 10 or 20min resulted in signicant reductions as com-
pared to those of fresh samples. Under atmospheric pressure, longer
heat application times (20 vs. 10 min) resulted in lower microbial
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 de-
stroys 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 previ-
ously observed (Pelczar, Chan, & Kreig, 1993), moist heat caused coagula-
tion 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. Ac-
cording 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 pretreat-
ment temperatures prior to application of high pressure. In earlier reports,
high pressures from 200 to 300MPa have been considered adequate to in-
activate vegetative cells of molds and yeast at ambient temperature
(Smelt, 1998), while there was complete eradication of microbial contam-
ination in meat subjected to 520 MPa for 1 h at 52 C after storage for
Microbial load (log cfu/g)
7 a Cooked control
6 0.1 MPa
Fresh
5
b b 200 MPa
4 c c
3
d
2
1 e e e e
0
Fresh Cooked T1 T2 T3 T4
control
Fig. 3. Aerobic plate count (log cfu/g meat) of duck skin-on whole breast muscle as a func-
tion 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

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 pro-
teins (San Martin, Barbosa-Cnovas, & Swanson, 2002), lack of ATP syn-
thesis and hydrolysis due to denaturation of enzymes (Farr, 1990),
interruption of cellular functions by decreasing the synthesis of ribo-
somes (Lado & Yousef, 2002), and disturbance of their membrane func-
tions (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 light-
ness (L*), yellowness (b*), hue angle (h), color distance (E) and white-
ness (W), but the lowest values for redness (a*) and chroma (C*). The
lower redness of cooked control samples was attributed to extended ex-
posure 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 sarco-
plasmic 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 pro-
cessing 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 signi-
cantly with pressure and heating times. High pressure accelerated the
changes occurring in the protein matrix of the meat system, so the pres-
sure treated samples achieved similar lightness as that of cooked control
at signicantly lower times and temperatures. The optical parameters of
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 be-
cause 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 signif-
icant 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 in-
creased 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, increas-
ing 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 ob-
served 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 mea-
surements (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 pretreat-
ment 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 tempera-
ture rose to 70 and 80C in heat-only and cooked control samples, respec-
tively, 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

Lightness Redness Yellowness Chroma Hue Color distance Whiteness

Cooked control 58.14 0.6a 13.42 3.05c 9.6 1.01a 16.65 2.06d 0.64 0.15a 60.51 0.6a 54.93 1.17a
(Cooked to a core temperature of 80 C)

0.1 MPa
Pre-treatment 10 C, then
70 C for 10 min 51.58 0.62d 19 1.03a 8.04 0.77cd 20.64 1.16ab 0.41 0.03cd 55.57 0.67d 47.36 0.78f
70 C for 20 min 55.29 0.73b 18.04 0.66ab 9.15 0.64ab 20.24 0.56abc 0.48 0.04bc 58.88 0.66b 50.93 0.75c
Pre-treatment 40 C, then
70 C for 10 min 53.1 0.73c 19.47 1.69a 7.91 0.55d 21.04 1.44a 0.4 0.05d 57.13 0.98c 48.59 0.73e
70 C for 20 min 55.29 0.74b 16.87 0.96b 9.05 0.87abc 19.16 1.07bc 0.5 0.04b 58.53 0.85b 51.36 0.71c

200 MPa
Pre-treatment 10 C, then
70 C for 10 min 53.52 0.65c 17.76 1.04ab 7.76 0.96d 19.41 0.97bc 0.42 0.06cd 56.94 0.78c 49.63 0.59de
70 C for 20 min 57.85 0.66a 16.6 1.06b 8.36 0.63bcd 18.6 1.02c 0.47 0.04bcd 60.78 0.76a 53.93 0.64b
Pre-treatment 40 C, then
70 C for 10 min 54.9 0.59b 17.96 1.58ab 8.66 0.71abcd 19.96 1.59abc 0.46 0.04bcd 58.44 0.77b 50.67 0.87cd
70 C for 20 min 58.26 0.91a 16.7 0.57b 9.07 0.66ab 19.01 0.66bc 0.51 0.03b 61.29 0.85a 54.14 0.92ab
1
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

Hardness Springiness Adhesiveness Cohesiveness Resilience Gumminess Chewiness

N - gs

Cooked control 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
(Cooked to a core temperature of 80 C)

0.1 MPa
Pre-treatment 10 C, then
70 C for 10 min 53.59 0.92c 0.62 0.01de 22.01 3.7bc 0.63 0.05bc 0.33 0.02a 33.38 2.22c 20.55 1.19d
70 C for 20 min 59.21 0.22b 0.64 0.01bc 31.07 4.61e 0.65 0.01ab 0.31 0.01b 38.23 0.54b 24.35 0.49b
Pre-treatment 40 C, then
70 C for 10 min 52.65 1.02c 0.62 0.01e 24.6 4.19cd 0.62 0.04c 0.33 0.03a 32.17 1.91c 19.72 1.05d
70 C for 20 min 58.72 1.28b 0.64 0.01bc 36 3.64f 0.63 0.02bc 0.31 0.01b 36.96 0.92b 23.49 0.71c

200 MPa
Pre-treatment 10 C, then
70 C for 10 min 33.7 0.64d 0.63 0.03cde 12.45 1.91a 0.61 0.02cd 0.34 0.02a 20.37 0.67d 12.72 0.16e
70 C for 20 min 30.1 1.16e 0.65 0.01b 19.93 1.75b 0.58 0.01de 0.29 0.01c 17.35 0.7e 11.23 0.47f
Pre-treatment 40 C, then
70 C for 10 min 33.47 0.79d 0.63 0.02cd 13.49 1.72a 0.61 0.02cd 0.33 0.01a 20.14 0.65d 12.65 0.54e
70 C for 20 min 30.21 0.61e 0.65 0.01b 23.74 2.32bcd 0.56 0.02e 0.28 0.01c 16.89 0.77e 10.88 0f
1
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 ten-
derness for samples heated under high pressure and heat than with
heat- or high pressure-alone. The low cohesiveness values of pressure-
heated 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 con-
trary, 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 in-
creased 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 indi-
cate 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.
3.7. Principal component analysis
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 en-
thalpies 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 en-
thalpies of sarcoplasmic and connective tissue being in the same
5
Denaturation
enthalpy of
actin
3
Slow-relaxation Slow-relaxation
proton times
compartment Total enthalpy
Fast-rexation of denaturation
1 times
F2 (34.76 %)

-5 -3 -1 1 3 5
The principal component analysis of denaturation enthalpies of sar- Fast-relaxation
-1 proton
coplasmic and connective tissue proteins and mobility and compart-
compartment
ment sizes of fast- and slow-relaxation protons in duck meat samples
subjected to high pressure and heat treatments is presented in Fig. 4.
Denaturation
The rst two principal components explained 80.28% of the total varia- -3 enthalpies of
tion occurring in the duck meat samples under heating and pressuriza- Sarcoplasmic
and connective
tion condition. The results revealed that a relationship existed between tissue proteins
denaturation enthalpies of protein and T2 relaxation values of protons
-5
in the myobrillar matrix and the modications in the protein struc-
F1 (45.52 %)
tures regulating the sizes of proton compartments. The placement of
fast and slow T2 relaxation times in the rst quadrant with denaturation Fig. 4. Relationship between denaturation enthalpies of proteins and mobility and com-
enthalpies of actin and total enthalpy of denaturation suggested the ex- partment sizes of fast- and slow-relaxation protons in duck meat samples subjected to
istence of relationships between these proteins on the mobility of water 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 treat-
ment in this study affected the protein contents of the duck meat
samples, which ultimately contributed to the changes in water mo-
bility 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 myo-
brillar 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 re-
sulted in improved tenderness and microbial safety at both treatment
times compared with the heat-only and cooked control samples. The op-
tical properties of pressure-heated samples at reduced temperatures and
times were comparable to those of the cooked control. The results indi-
cated 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. Follow-
up 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 com-
position, 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 ox-
idative 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 ad-
dition 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
Fernandez-Martin, F. (2007). Bird muscles under hydrostatic high-pressure/temperature
combinations. Journal of Thermal Analysis and Calorimetry, 87(1), 285290.
Fernndez-Martn, F., Fernndez, P., Carballo, J., & Colmenero, F. J. (1997). Pressure/heat
combinations on pork meat batters: Protein thermal behavior and product rheologi-
cal properties. Journal of Agricultural and Food Chemistry, 45(11), 44404445.
FernndezMartn, F., Otero, L., Solas, M., & Sanz, P. (2000). Protein denaturation and
structural damage during high-pressure-shift freezing of porcine and bovine muscle.
Journal of Food Science, 65(6), 10021008.
Ferrini, G., Comaposada, J., Arnau, J., & Gou, P. (2012). Colour modication in a cured meat
model dried by Quick-Dry-Slice process and high pressure processed as a function
of NaCl, KCl, K-lactate and water contents. Innovative Food Science and Emerging
Technologies, 13, 6974.
FSANZ (2001). Guidelines for the microbiological examination of ready-to-eat foods. Food
Science Australia and New Zealand, Vol. 2012.
Jeremiah, L., & Gibson, L. (2003). Cooking inuences on the palatability of roasts from the
beef hip. Food Research International, 36(1), 19.
Jimnez Colmenero, F. (2002). Muscle protein gelation by combined use of high
pressure/temperature. Trends in Food Science and Technology, 13(1), 2230.
Kruk, Z. A., Yun, H., Rutley, D. L., Lee, E. J., Kim, Y. J., & Jo, C. (2011). The effect of high pres-
sure on microbial population, meat quality and sensory characteristics of chicken
breast llet. Food Control, 22(1), 612.
Lado, B. H., & Yousef, A. E. (2002). Alternative food-preservation technologies: Efcacy
and mechanisms. Microbes and Infection, 4(4), 433440.
Lee, E. J., Kim, Y. J., Lee, N. H., Hong, S. I., & Yamamoto, K. (2007). Differences in properties
of myobrillar proteins from bovine semitendinosus muscle after hydrostatic pres-
sure or heat treatment. Journal of the Science of Food and Agriculture, 87(1), 4046.
Li, C., Liu, D., Zhou, G., Xu, X., Qi, J., Shi, P., et al. (2012). Meat quality and cooking attributes
of thawed pork with different low eld NMR T21. Meat Science, 92(2), 7983.
Li, C. T., & Wick, M. (2001). Improvement of the physicochemical properties of pale soft
and exudative (PSE) pork meat products with an extract from mechanically deboned
turkey meat (MDTM). Meat Science, 58(2), 189195.
Liu, Y., Xu, X. -l, & Zhou, G. -h (2007). Changes in taste compounds of duck during process-
ing. Food Chemistry, 102(1), 2226.
Ma, H. J., & Ledward, D. (2004). High pressure/thermal treatment effects on the texture of
beef muscle. Meat Science, 68(3), 347355.
Marcos, B., Kerry, J. P., & Mullen, A.M. (2010). High pressure induced changes on sarco-
plasmic protein fraction and quality indicators. Meat Science, 85(1), 115120.
Montiel, R., De Alba, M., Bravo, D., Gaya, P., & Medina, M. (2012). Effect of high pressure
treatments on smoked cod quality during refrigerated storage. Food Control, 23(2),
429436.
Moure, A., Sineiro, J., Domnguez, H., & Paraj, J. C. (2006). Functionality of oilseed protein
products: A review. Food Research International, 39(9), 945963.
Pagn, R., & Mackey, B. (2000). Relationship between membrane damage and cell
death in pressure-treated Escherichia coli cells: Differences between exponential-and
stationary-phase cells and variation among strains. Applied and Environmental
Microbiology, 66(7), 28292834.
Paidhungat, M., Setlow, B., Daniels, W. B., Hoover, D., Papafragkou, E., & Setlow, P. (2002).
Mechanisms of induction of germination of Bacillus subtilis spores by high pressure.
Applied and Environmental Microbiology, 68(6), 31723175.
Palka, K., & Daun, H. (1999). Changes in texture, cooking losses, and myobrillar structure
of bovine M. semitendinosus during heating. Meat Science, 51(3), 237243.
Pearce, K. L., Rosenvold, K., Andersen, H. J., & Hopkins, D. L. (2011). Water distribution and
mobility in meat during the conversion of muscle to meat and ageing and the impacts
on fresh meat quality attributes A review. Meat Science, 89(2), 111124.
Pelczar, M. J., Chan, E. G., & Kreig, N. R. (1993). Microbial growth. Microbiology: Concepts
and applications (pp. 175198). New York: McGraw-Hill Inc.
Pereira, R. N., & Vicente, A. A. (2010). Environmental impact of novel thermal and
non-thermal technologies in food processing. Food Research International, 43(7),
19361943.
Ramirez-Suarez, J. C., & Morrissey, M. T. (2006). Effect of high pressure processing (HPP)
on shelf life of albacore tuna (Thunnus alalunga) minced muscle. Innovative Food
Science and Emerging Technologies, 7(12), 1927.
San Martin, M., Barbosa-Cnovas, G., & Swanson, B. (2002). Food processing by high hy-
drostatic pressure. Critical Reviews in Food Science and Nutrition, 42(6), 627645.
Sikes, A. L., Tobin, A.B., & Tume, R. K. (2009). Use of high pressure to reduce cook loss and
improve texture of low-salt beef sausage batters. Innovative Food Science and Emerging
Technologies, 10(4), 405412.
Sikes, A., Tornberg, E., & Tume, R. (2010). A proposed mechanism of tenderising post-rigor
beef using high pressureheat treatment. Meat Science, 84(3), 390399.
Simonin, H., Duranton, F., & de Lamballerie, M. (2012). New insights into the highpressure
processing of meat and meat products. Comprehensive Reviews in Food Science and Food
Safety, 11(3), 285306.
Smelt, J. (1998). Recent advances in the microbiology of high pressure processing. Trends
in Food Science and Technology, 9(4), 152158.
Sun, X. D., & Holley, R. A. (2010). High hydrostatic pressure effects on the texture of meat
and meat products. Journal of Food Science, 75(1), R17R23.
Tseo, C., Deng, J., Cornell, J., Khuri, A., & Schmidt, R. (2006). Effect of washing treatment on
quality of minced mullet esh. Journal of Food Science, 48(1), 163167.
USDA-FSIS (2012). Chicken from farm to table. Poultry Preparation, Vol. 2012.
Villamonte, G., Simonin, H., Duranton, F., Chret, R., & de Lamballerie, M. (2012). Functionality
of pork meat proteins: Impact of sodium chloride and phosphates under high-pressure
processing. Innovative Food Science and Emerging Technologies, 18, 1523.
Yuste, J., Mor-Mur, M., Capellas, M., Guamis, B., & Pla, R. (1999). Mechanically recovered poul-
try meat sausages manufactured with high hydrostatic pressure. Poultry Science, 78(6),
914921.