Research Article

Received: 8 March 2010

Revised: 19 September 2010

Accepted: 30 September 2010

Published online in Wiley Online Library:

(wileyonlinelibrary.com) DOI 10.1002/jsfa.4204

Influence of heat on protein degradation,

ultrastructure and eating quality indicators
of pork
Feng Huang, Ming Huang, Xinglian Xu and Guanghong Zhou
Abstract
BACKGROUND: Heating temperature is an important factor affecting meat palatability. This study aimed to evaluate the
influence of heating temperature on some eating quality indicators, protein degradation and ultrastructure of pork muscle
fibres and their correlations.
RESULTS: Cooking loss (CL) increased gradually (P < 0.05) with increasing temperature.
Warner Bratzler shear force (WBSF)

increased
in two separate phases from 25 to 50 C and again from 60 to 100 C (P < 0.05), with a steady phase from 50

to 60 C (P > 0.05); conversely, a significant increase in pH (P< 0.05) occurred

between
50 and 60 C. Strong correlations
(P < 0.01) among pH, CL, WBSF and colour parameters L
and b were observed following the heating process.
Increasing
temperature
induced
gradual
degradation
of
many
muscle
proteins,
but
myosin
was not significantly degraded

until 80 C and
actin showed no visible degradation throughout the whole heating process. Meanwhile, the structure of muscle fibres also
changed significantly on heating, with sarcomeres contracting transversely and longitudinally and becoming condensed, but
there was no occurrence of breakage within fibres.
CONCLUSION: Heating temperature has a great effect on eating quality indicators, protein degradation and ultrastructure of
pork muscle fibres.
c 2010 Society of Chemical
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Keywords: Jinhua pork; temperature; eating quality; protein degradation; ultrastructure

INTRODUCTION
It is well known that cooking is an essential process to achieve
palatable and safe meat products.1 However, cooking of meat
also leads to a decrease in its nutritional value, mainly resulting
from vitamin and mineral losses.2,3 Consequently, maintaining
a balance of multiple quality attributes is a requisite in the
processing of cooked meat. Currently, factors affecting eating
quality of meat in the cooking process mainly include cooking
time, temperature and cooking method. Numerous new
techniques (such as microwave, far-infrared radiation and
ultrasound cooking) have been employed to cook meat, but
cooking in water, a universal process in industry and
households for its economy and simplicity, is also of
significance and is believed to be a reliable method to
optimise tenderness owing to rapid and more consistent increases
in internal temperature.4
It is well documented that the final internal temperature has a
great effect on ultimate palatability, as assessed by a combination
of colour, tenderness, flavour, water-holding and juiciness.5 7
Further, the final temperature is considered to be important for
structural changes such as transverse and longitudinal shrinkage
of muscle fibres due to meat protein denaturation during the
cooking process. Cooking has also been defined as the heating of
meat to a sufficiently high temperature to denature proteins.8
Muscle proteins, accounting for approximately 200 g kg1
muscle, are of great significance for the maintenance of meat
product structure. Basically they can be divided into three groups,
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namely myofibrillar (salt-soluble), sarcoplasmic (water-soluble)

and connective tissue (insoluble) proteins. Myofibrillar proteins,
the main component of muscle proteins (ca 550 600 g
kg1 total proteins), can be further subdivided into three
classes,
i.e. structural proteins (myosin, actin, etc.), which build up the
main structure of muscle, regulatory proteins (troponin, etc.) and
cytoskeletal proteins (titin, nebulin, desmin, etc.), which support
the whole myofibrillar structure. However, sarcoplasmic proteins
mainly include enzymes involved in energy metabolism. Collagen
is the main component of connective tissue proteins and is
located extracellularly. Previous studies have revealed that
sarcoplasmic

proteins aggregate between 40 and 60 C9 and that myosin

and

actin denature at temperatures lower than 50 C and higher

than

65 C respectively.10
However, the majority of the reported researches were focused
on a few changing traits of meat separately induced by heating,
and little work has been done on relationships among
characteristics of

Correspondence to: Ming Huang, Key Laboratory of Meat Processing

and Quality Control, Ministry of Education, College of Food Science and
Technology, Nanjing Agricultural University, Nanjing 210095, China.
E-mail: mhuang@njau.edu.cn

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Key Laboratory of Meat Processing and Quality Control, Ministry of

Education, College of Food Science and
Technology, Nanjing
Agricultural University, Nanjing 210095, China

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eating quality and between eating quality and protein
degradation and structure of muscle fibres. The objectives of this
study were to evaluate the effect of heat treatment on pH,
colour, cooking loss, Warner Bratzler shear force, protein
degradation and structure of muscle fibres and their correlations.

MATERIALS
METHODS

F Huang et al.

C
o
l
o
u
r
The colour of heated meat samples was expressed in
terms of L (lightness), a
(redness) and b
(yellowness) values determined using a Minolta CR400 Chroma Meter (Japan). For each sample, three
measurements were made at internal locations and
the

AND

Meat samples and heating process

Eight Jinhua pigs were slaughtered humanely at Qinglian slaughterhouse (Zhejiang, China) according to standard procedures.
Following chilling for 24 h, longissimus dorsi muscles (from 12th
thoracic vertebrae to 5th lumbar vertebrae) were removed from
both sides of each carcass. Each longissimus muscle was trimmed
of
visible fat and connective tissue and cut into five 70 mm 45
mm
25 mm (length width thickness) pieces. After
weighing
accurately with an electronic balance (JA 2003, Hangping, Shanghai, China) and measuring the length, width and thickness using
vernier calipers, samples were placed in vacuum bags (unsealed)
and heated to one of five designated internal temperatures (25,

50, 60, 80 or 100 C) in a water bath. Upon reaching the

designated
temperature, samples were kept in the water bath for 5 min.
These meat samples were used for subsequent analyses.
Thermocou- ples (UA-920C, Uygao, Shanghai, China) were
inserted into the geometric core of each steak to monitor the
internal temperature.
pH
The pH values of heated meat samples were measured with
a digital pH meter (Hanna, Italy). Approximately 4 g of
minced meat sample was homogenised with 36 mL of pre-cooled
distilled water in a polytron at a speed of 15 000 rpm for
10 s. After equilibration to room temperature the pH was
recorded. Each sample was measured in triplicate to calculate
the average value as the final pH.
Cooking loss
Samples were removed from the vacuum bags and cooled to room
temperature. Superficial water was absorbed using blotting
paper, then each sample was accurately weighed. Cooking loss
(CL) was calculated as
CL (%) = [(raw weight cooked weight)/raw weight] 100
(1)
Texture
After determination of cooking losses, heated samples were

chilled at 4 C for 24 h, then six 1.27 cm diameter cores were

removed from each sample parallel to the muscle fibre
orientation. Each
core was sheared through once using a Warner Bratzler
shear machine (235G-R, Manufacturing Co., UK), and Warner
Bratzler
shearaveraged
force (WBSF)
data were recorded.
values were
and recorded.

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Protein extraction and sample preparation

For extraction of sarcoplasmic proteins, approximately 1.5 g of minced
meat sample was homogenised with 150 mL of extraction buffer containing
10 mmol L1 ethylene diamine tetraacetic acid
(EDTA) and 50 mmol L1 Tris (pH 8.3) in a polytron at a speed of
13 000 rpm for 10 s. This was repeated a further twice, with a 15 s cooling
period between bursts. The homogenate was centrifuged

at 15 000 g for 30 min at 4 C and the supernatant was collected

as sarcoplasmic proteins.
Myofibrillar proteins were extracted according to the proce- dure of
Etlinger et al.11 with some modifications. The pellet from sarcoplasmic
protein extraction was homogenised with approxi- mately 7.5 volumes of
pyrophosphate relaxing buffer (PRB) buffer
(100 mmol L1 KCl, 2 mmol L1 MgCl2 , 2 mmol L1 ethylene glycol tetraacetic acid, 1 mmol L1 dithiothreitol, 1 mmol L1 NaN3 ,
2 mmol L1 Na4 P2 O7 , 10 mmol L1 Tris-maleate, pH 6.8) in a polytron at a speed of 13 000 rpm for 10 s and the homogenate was centrifuged
at 1000 g for 10 min. The pellet was subsequently
washed eight times, each wash with 10 volumes of low-salt buffer
(same as PRB except for pyrophosphate being omitted). In the final step the
myofibrils were suspended in Tris-EDTA buffer
(10 mmol L1 Tris, 5 mmol L1 EDTA, pH 8).
The concentrations of sarcoplasmic and myofibrillar proteins were
determined with a BCA Protein Assay Kit (Pierce, America). Samples were
then mixed with treatment buffer (125 mmol L1
Tris, 40 g L1 sodium dodecyl sulfate (SDS), 250 g L1 glycerol), heated at

50 C for 20 min and finally stored at 80 C for

subsequent SDS polyacrylamide gel electrophoresis (SDS-PAGE).
SDS-PAGE
A 50 g L1 polyacrylamide
continuous
gel
(acrylamide/
bisacrylamide
100 : 1 w/w,
1 g L1
SDS,
0.5 g L1
tetramethylethylenediamine (TEMED), 1 g L1 ammonium persulfate (APS), 2
mmol L1 EDTA, 200 mmol L1 Tris-HCl, pH 8) was used for determination
of myofibrillar proteins (mainly high-molecularweight proteins). Two 125 g L1 polyacrylamide separating gels
(acrylamide/bisacrylamide 37.5 : 1 w/w, 1 g L1 SDS, 0.37 g L1
TEMED, 0.5 g L1 APS, 0.5 mol L1 Tris-HCl, pH 8.8) were used to detect
changes in myofibril and sarcoplasmic proteins respectively. A 40 g L1 polyacrylamide gel was used as stacking gel. The running
buffer contained 25 mmol L1 Tris, 192 mmol L1 glycine
and 1 g L1 SDS (pH 8.3). The 50 and 125 g L1 gels were run on
a Bio-Rad Mini-Protean II system (Bio-Rad Laboratories, Hercules, CA, USA) at
a constant current setting of 5 mA per gel for 18 h and at a constant
voltage of 120 V for approximately 2.5 h respec- tively. After electrophoresis,
gels were stained for 1 h in an excess
of 1 g L1 Coomassie brilliant blue R-250, 316 g L1 ethanol and
73 g L1 glacial acetic acid and then destained in an excess of the same
solution without the Coomassie brilliant blue R-250. Gels were scanned
(GT-800F, Epson, Japan) at a resolution of 600 dpi.
Muscle ultrastructure
Samples were cut into 2 mm 3 mm 10 mm pieces and fixed

overnight at 4 C by immersion in 100 g L1 pre-cooled glutaraldehyde

1
in 0.1 mol L
phosphate buffer solution (PBS,
pH 7.4). Afterwards, samples were rinsed with PBS, post-fixed in 10 g
L1 osmium tetroxide for 3 h, dehydrated in ethanol, exchanged in
propylene oxide and embedded in Spurrs resin. Ultrathin sections were
stained with uranyl acetate and lead
citrate and examined by transmission electron microscopy (H-

values were averaged and recorded.

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Heat effects on ultrastructure and eating quality of pork

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Table 1. Values of pH, cooking loss (CL), Warner Bratzler shear force (WBSF) and colour (L , a and b ) of cooked pork longissimus at
different internal temperatures
Internal temperature ( C)
Parameter

25

pH
CL (%)
WBSF (kg)
Colour

5.63
0.93
2.31
48.46
5.99
2.30

L
a
b

50
0.11a
0.31a
0.38a
1.13a
0.89a
0.26a

5.76
7.38
4.06
72.18
9.26
8.21

60
0.12a
1.55b
0.29b
2.81b
0.59c
0.71b

5.95
16.90
4.09
77.89
8.03
9.67

80
0.06b
1.93c
0.07b
0.64d
0.56b
0.79c

5.96
35.70
7.67
77.19
5.38
10.33

100
0.08b
1.34d
1.13c
0.42cd
0.35a
0.34cd

P value

6.05 0.12b
41.37 0.31e
8.68 0.15c
75.10 0.42c
5.32 0.44a
10.66 0.17c

1.82524
3.99139
1.46689
3.49700
1.79535
1.99534

104
1017
108
1014
107
1012

Values are mean standard deviation. Means with the same letter in a row are not different at 95% level.

Statistical analysis
The data from 16 replicates were analysed using SPSS software
(SPSS Inc., Chicago, IL, USA). Differences among individual means
were compared by Duncans multiple range test. Correlation
analysis was conducted using the bivariate test. Effects were
considered significant at P < 0.05.

RESULTS
pH
Heating temperature had a significant effect on pH (P < 0.01)
(Table 1). As internal temperatures increased, pH values increased
consistently, which is in agreement with previously reported
results.12 However, changes in pH at different temperature phases
were not different. According to Duncans multiple comparison
test, a significant difference (P < 0.05) was detected only
between

50 and 60 C, while increases in pH between 25 and 50 C

and

between 60 and 100 C were not significant (P > 0.05).

0.05). With increasing temperature, a values increased significantly up

to

50 C (P < 0.05) but then decreased markedly between 50 and

80 C (P < 0.05), with no change between 80 and 100 C (P > 0.05).

Cooking loss
The results for CL of meat samples are presented in Table 1. The
final core temperature of the meat had a significant effect on
CL (P < 0.01), which increased significantly with increasing core

temperature and reached approximately 41% at 100

C.
Texture
The final internal temperature of the meat also had a large impact
on WBSF (Table 1). As the core temperature increased, WBSF of
meat increased significantly (P < 0.05) in two separate phases

from 25 to 50 C and again from 60 to 100 C, with little

change

(P > 0.05) between 50 and 60

C.
Colour
Heating had a great impact on the colour of meat (Table 1).

As the core temperature increased from 25 to 60 C, values

for L
increased
(P < 0.05), reaching a peak (77.89) at 60

C. Above 60 C, L values decreased slightly.

Values for b

increased significantly between 25

and
60
C
(P
< 0.05) and

continued to increase above 60 C, but not significantly (P >

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Table 2. Correlation coefficients among pH, cooking loss (CL),

Warner Bratzler shear force (WBSF) and colour (L , a and b
) of cooked pork longissimus during cooking process
pH

Correlation analysis for heating pH, CL, WBSF

and colour
The results of correlation analysis for pH, CL, WBSF
and colour are presented in Table 2. Strong
correlations (P < 0.01) among pH, CL, L and b were
observed during the cooking process. Values for a
only showed significant correlations with CL and WBSF
(P < 0.05).

CL

WBSF

pH
1.000
CL
0.772 1.000
WBSF 0.752 0.943 1.000
L
0.706 0.666 0.622
a
0.211
0.559 0.491

b
0.784
0.789 0.759

P < 0.05;

1.000
0.156
0.963

1.000
0.028

1.000

P < 0.01.

Degradation
of
muscle proteins
As the temperature of the core increased,
sarcoplasmic proteins were gradually degraded (Fig.

1(a)). At 50 C, protein bands with a molecular

weight of ca 100 kDa disappeared, the content of
proteins with a molecular weight of ca 43 44
kDa distinctly
decreased but the content of other proteins increased.

At 60 C the content of proteins (possibly myoglobin)

with a molecular weight of ca 34 kDa increased
continuously but other protein bands became weak

and even disappeared. At 80 C, all sarcoplasmic

protein bands became weak or disappeared. No
visible change in any of the protein bands was

observed between 80 and 100 C. Overall, the

degradation of many sarcoplasmic proteins occurred

between 50 and 60 C.
Myofibrillar proteins had greater thermal stability
than sar- coplasmic proteins (Figs 1(b) and 1(c)). As
the core temperature increased, the density of
myosin heavy chain (MHC) remained almost

unchanged at temperatures up to 80 C but

decreased significantly at 100 C (Fig. 1(b)). Little

visible change occurred in the density of actin (Fig.

1(b)) in the temperature range 25 100 C. Protein

bands with molecular weights of ca 15 and 47 60

kDa appeared at 60 C and their densities increased

with increasing
internal temperature. Using 50 g L1 continuous
SDS-PAGE gels, we found that nebulin was not altered

up to 60 C but was slightly degraded at 80 C and

completely disappeared at 100 C (Fig. 1(c)).

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F Huang et al.

Figure 1. Representative electrophoresis

of Coomassie-stained polyacrylamide gels depicting degradation of muscle proteins at different internal
temperatures: (a) 125
g L1 gels loaded with 20 g sarcoplasmic protein samples; (b) 50 g L1 gels loaded with 80 g myofibrillar protein
samples; (c) 125 g L1 gels loaded with 20 g myofibrillar protein samples; Std, molecular standards, A, B, C, D and E, meat samples at 25, 50, 60, 80
and 100 C
respectively; MHC, myosin heavy chain.

importance to the catering industry, which primarily

sells meat that has been

Little difference in titin degradation was observed below 50 C,

but titin was completely degraded beyond 60 C (Fig. 1(c)).

Muscle ultrastructure
The final heating temperature had a large influence on the

ultrastructure of pork muscles. At 25

C the structure of
myofibrils was regular and aligned and clearly perceived
with intact Z lines, I bands and A bands (Fig. 2(a)). As the
core temperature increased, changes in the structure of
muscle fibres occurred progressively, with the I bands
becoming shortened and more condensed (Figs 2(b) and 2(c)).
However, the A bands appeared slightly stretched and the M
lines became ambiguous between

50 and 60 C and were difficult to distinguish at 80 C and

above. Z lines were clearly evident throughout the whole heating
range,
but some
breaks were observed near the Z lines at temperatures

of 80 C and above (Figs 2(d) and 2(e)).

DISCUSSION
Raw meats are usually cooked to make them acceptable to
potential consumers. This is because cooking affects many
attributes of eating quality through multiple physicochemical
changes, and these attributes usually include tenderness, colour,
appearance and cooking loss. Therefore it is important to
understand the changes in physicochemical properties and eating
quality during heating.
Weight loss through loss of moisture during cooking is an issue
of concern to people, because it not only affects a products final
appearance
is also of
economic
cooked. In ourand
study,juiciness
cooking but
loss increased
withgreat
increasing
core

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heating in a water bath gives rise to low cooking loss.19

This

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temperature, and this trend became more pronounced in the range 60

100 C. An increase in cooking loss with increasing internal

temperature has also been observed in beef13 and rabbit
meat,6 but the results of Combes et al.6 showed a constant cooking

loss between 80 and 90 C. This phenomenon was not observed in the

present study and may result from a higher water-holding capacity of
rabbit meat.14 Cooking loss generally includes a combination of liquid
and soluble matter lost from meat during cooking, the main component
being water.15 The majority of water in meat is held within the
structure of the muscle and muscle cells.16 Therefore the loss of water
during cooking is caused by the destruction of structures of muscle cells due
to the denaturation of myofibrillar proteins by heat. It has been
documented that changes in sarcomere length and cooking loss are
inversely proportional.17 In this study, sarcomere length shortened with
increasing temperature, particularly when core temperatures increased

from 50 to 80 C, and this is consistent with the loss of water on heating.

Results on transverse tissue morphology under optical microscopy also
showed that myofibril
fibre density increased significantly, doubling after 15 min of heating at
100 C.18 Although significant shrinkage of myofibrils
occurred on heating, unlike the structural changes of myofibrils observed
during post mortem tenderisation of meat, there was no occurrence of
apparent breaks in myofibrils throughout the whole heating process in our
study, which suggested that even though muscle proteins were degraded
on heating, they were still located in their original position with no apparent
translocation. In addition to temperature, different heating methods
(microwave, water bath, etc.) could also result in different cooking
losses. Compared with the popular method of microwave heating,

cooked. In our study, cooking loss increased with increasing core

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heating in a water bath gives rise to low cooking loss.19

This

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Figure 2. Representative transmission electron micrographs showing changes in muscle ultrastructure at internal temperatures of (a) 25, (b) 50, (c) 60,
(d) 80 and (e) 100 C. Scale bar: 1 m.

is likely due to the fact that microwaves cause a fast temperature

rise in foods owing to their capacity to generate heat energy
inside the food without requiring any medium as vehicle for heat
transfer, which does not occur in conventional heating, and a high
temperature even for a short time will create a large area of spaces
within the myofibrillar mass, which is positively correlated with
cooking loss.18 Yarmand and Homayouni20 have also reported that
domestic microwave cooking causes more damage to the structure
of both the connective tissue and the myofibrillar elements than
conventional heating.
In addition, the net charge of muscle proteins may affect the
retention of water through interactive forces between charges.16
In our study, pH values increased gradually with increasing
temperature (Table 1), which may be attributed to the loss of
free acidic groups,21 thus influencing cooking loss. Meanwhile, a
significant inverse correlation (P < 0.01) between cooking loss
and pH was also observed (Table 2). In our study a significant
increase

in pH only occurred between 50 and 60 C and the majority of

sarcoplasmic proteins were degraded at the same temperature
phase; therefore the change in pH value of meat during heating
was likely a result of the dynamic balance of acid base groups
at the surface of sarcoplasmic proteins.
Tenderness is rated as the most important eating quality
characteristic of meat by consumers.22 Therefore influences
of cooking on meat tenderness have received considerable
attention. It is known
that
heating
can strengthen
myofibrillar protein networks, which leads to toughening, but at
the same time may solubilise connective tissue, leading to
tenderisation. The decrease in meat tenderness is generally
observed in two distinct phases:

between 40 and 60 C and between 65 and 80 C.8,23

Bouton
and Harris23 attributed the first increase in meat toughness
to connective
tissue denaturation and the second
to
denaturation
of myofibrillar proteins. However, Davey and Gilbert8 offered
J Sci Food Agric
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the opposite interpretation and attributed the first increase in

meat toughness to denaturation of myofibrillar proteins and the

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second to connective tissue denaturation. In our study, increase

in toughness was also observed in two separate phases
from

25 to 50 C and again from 60 to 100 C. It is widely

accepted
that
shrinkage of sarcomeres due to denaturation of
myofibrillar proteins could cause an increase in toughness. In
our study, there was no change in toughness at temperatures
between 50 and

60 C, which differs from the findings of Christensen et al.,24

who
observed a decrease in meat toughness for the same
temperature interval and attributed it to collagen solubilisation.
This is possibly because the longissimus dorsi muscle used in
our study has a relatively low collagen content compared with
the semitendinosus muscle used by Christensen et al.24 In
addition, heating method is also an important factor affecting
the tenderness of meat. For example, the tenderness of meat
heated in a water bath is better than that of microwave-heated
meat,19 which may be due to the higher loss of water from
muscle during microwave heating resulting in greater hardening
of myofibrillar proteins.
Meat colour is an important trait of eating quality in that
consumers use colour in their decision process to purchase
meat as it is considered to be an indicator of meat
freshness. Meat colour is also used by consumers as an
indicator of the degree of doneness.25 During cooking,
meat
becomes progressively browner from its initial red
colouration. Objective
colour measurements confirmed the visual findings: L , a and
b
values increased significantly as the core temperature increased

between 25 and 50 C; at core temperatures above 50 C,

with increasing core temperature, L values did not change

significantly, a values decreased and b values increased
consistently. These results differed somewhat from previous
findings.26,27 However, a and b values changed more
significantly at temperatures below

50 C, which may be due to the higher pH values at

internal temperatures greater than 50 C, since higher pH

decreases
denaturation of myoglobin and thus change in colour. Although
meat colour is closely related to temperature, visual appraisal
of cooked colour by consumers, who use brown colour of meat
as

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an indicator of doneness, is not a completely reliable indicator.
For example, premature browning was found to occur owing to
the presence of oxymyoglobin and metmyoglobin in meat at the
time of cooking;28 moreover, some researchers observed that
beef

patties remained pink when cooked to 74 C or higher.29

CONCLUSION
In summary, the heating temperature has a significant effect
on pH, CL, WBSF, colour, degradation of muscle proteins
and ultrastructure of muscle fibres. With increasing internal
temperature, CL increased gradually (P < 0.01), while WBSF

increased in two separate phases from 25 to 50 C and again

from

60 to 100 C (P < 0.05), with a stable phase from 50 to 60 C (P

>
0.05); conversely, a significant increase in pH (P < 0.05) occurred

between 50 and 60 C. Strong correlations (P < 0.01) among CL,

pH, L and b were observed during the cooking process.
With
increasing temperatures, degradation of many muscle proteins
occurred gradually. However, myosin remained unchanged below

80 C and then was degraded rapidly, whereas actin showed no

visible change at any of the temperatures investigated.
Meanwhile, the visual appearance of the muscle fibre
structure changed significantly on heating, with sarcomeres
contracting transversely and longitudinally and becoming
condensed, but there was no occurrence of breakage within
fibres.

ACKNOWLEDGEMENTS
This research was funded by the National Natural Science Foundation of China (30972133) and the Natural Science Foundation of
Jiangsu Province (BK2009314).

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