ENGINEERING/PROCESSING
Apparent Specific Heat of Chicken Breast
Patties and their Constituent Proteins by
Differential Scanning Calorimetry
R.Y. MURPHY, B.P. MARKS, and J.A. MARCY
ABSTRACT
Chicken breast meat yielded three endothermic transitions,
with peak transition temperatures of 53, 70, and 79°C. Com-
parison with the purified protein fractions indicated that these
transitions corresponded to denaturation of myofibrillar
(53°C) and sarcoplasmic (70 and 79°C) proteins. The appar-
ent specific heat profile of chicken breast meat was suc-
cessfully modeled as a weighted average of the apparent
specific heat of the constituent proteins. The specific heats
of sarcoplasmic protein, myofibrillar protein, and chicken
breast meat were strongly influenced by temperature; how-
ever, the specific heat of stromal protein was nearly constant
across the temperature range considered (i.e., 10 to 100°C).
Key Words: poultry, protein, denaturation, specific heat,
differential scanning calorimetry
INTRODUCTION
IN DESIGNING THERMAL PROCESSING SYSTEMS FOR THE FOOD
industry, one of the most important limitations is the lack of quantita-
tive data on thermal properties (de dios Alvarado, 1991). Rizvi et al.
(1993) noted that the lack of data in this area has limited the application
of many well-established engineering principles. In order to properly
design a continuous thermal process for any food product, it is neces-
sary to calculate the energy requirements.
In particular, specific heat (cp) indicates the energy required to
change the temperature of a unit mass of material. Specific heat mea-
surements have been reported for various foods, including flat bread
(Gupta, 1990), fruit pulp (de dios Alvarado, 1991), vegetable juice
(Choi and Okos, 1983, 1986), bovine and soy milk (Oguntande and
Akintoye 1991), pork/soy hull mixture (Muzilla et al., 1990), seafood
(Rahman, 1993), wheat, rice and oats (Hwang and Hayakawa, 1979),
apples (Ramaswamy and Tung, 1981), and fat (Polley et al., 1980).
However, only calculated data were found for the cp of poultry prod-
ucts (Polley et al, 1980; ASHRAE, 1985).
Most cp models for food systems are functions of only water
content (de dios Alvarado, 1991; Gupta, 1990). However, the cp’s of
proteins, fats, and carbohydrates differ from one another and there-
fore have variable effects on the cp of a composite food material
(Sweat, 1995). Some models include different components of the
food and express cp as a linear combination of the cp’s of water, fat,
protein, carbohydrate, and/or ash (Oguntunde and Akintoye, 1991;
Rahman, 1993). However, the cp’s of each component may depend on
the source; different types of proteins from the same raw material may
have different cp’s.
For protein foods in general, most published data were measured
at a specific temperature and for a composite product (McProud and
Lund, 1983; Rahman, 1993; Oguntunde and Akintoye, 1991; Polley,
1980). However, muscle proteins are generally categorized as sarco-
plasmic, myofibrillar, or stromal, based on solubility. Differences in
thermal properties, such as gelation, have been reported for the vari-
Authors Murphy and Marks are with the Dept. Of Biological & Agricultural Engi-
neering, 203 Engineering Hall, Univ. of Arkansas, Fayetteville, AR 72701. Author
Marcy is with the Dept. of Poultry Science, Univ. of Arkansas, Fayetteville, AR 72701.
Address inquiries to Dr. B.P. Marks.
88 JOURNAL OF FOOD SCIENCE—Volume 63, No. 1, 1998
ous protein fractions in pork meat (Lan et al., 1995). However, no
information has been published regarding the effects of temperature
on the cp’s of chicken meat proteins.
The most commonly used methods for determining cp are the
method of mixtures and differential scanning calorimetry (DSC). The
advantages of DSC are that measurements are rapid, multiple data can
be obtained from a single thermogram, and a very small sample can
yield accurate results (Wang and Kolbe, 1991). DSC is the only meth-
od for direct determination of enthalpy associated with changes in
protein state (Wang and Smith, 1994), and it has been applied to study
protein denaturation in various other food systems (Bertola et al.,
1994; Relkin, 1994; Riva and Schiraldi, 1994; Ma and Harwalkar,
1991; Stabursvik and Martens, 1980). Specifically, Wright et al. (1977)
reported DSC transitions for both whole muscle and the component
proteins of rabbit meat. Kijowski and Mast (1988a) related the ther-
mal transitions of breast, thigh, blood, and skin tissues of chicken
broilers to the denaturation of isolated protein fractions. Xiong and
Brekke (1990) studied the thermal denaturation of extracted salt-solu-
ble proteins from pre- and postrigor chicken muscle. Xiong et al.
(1987) evaluated thermal denaturation of chicken breast and thigh
muscle proteins from certain whole broiler carcasses. However, no
detailed data have been published on the thermal properties of com-
mercially processed chicken meat products.
Our overall research program is aimed at improving methods for
design and control of thermal processing systems in the poultry in-
dustry. Models are being developed to predict product temperature,
moisture content, physicochemical quality, and microbial destruction
during thermal processing. In order to optimize the accuracy and util-
ity of these models, there is a strong need for data on fundamental
thermal properties of poultry meat. Consequently, our specific objec-
tive was to quantify the denaturation temperatures, denaturation en-
thalpies, and apparent specific heat of chicken breast meat and its
constituent proteins, as related to temperature.
MATERIALS & METHODS
Compositional analysis
Ground, formed, and frozen chicken breast patties (~53g each) were
obtained from a commercial processor. For raw compositional analysis,
20 chicken breast patties were thawed 12h at 4°C. Crude fat, moisture,
and protein contents were determined by AOAC procedures, sections
24.005, 24.002, and 24.027, respectively (AOAC, 1984).
Sarcoplasmic, myofibrillar and stromal proteins
Sarcoplasmic, myofibrillar, and stromal proteins were prepared
using the procedures described by Lan et al. (1995), with modifica-
tions as follows. Unless specified otherwise, all preparations were
conducted at 4°C. A buffer solution of 0.05M NaCl, 0.05M potassi-
um phosphate, 1 mM EDTA, and 1 mM NaN3 at pH 7.0 was used to
extract sarcoplasmic proteins. The extracted sarcoplasmic fractions
were dialyzed against deionized water for 24h twice, and freeze-dried.
The myofibrillar proteins were washed with deionized water 6 times
before being freeze-dried. The stromal proteins were washed using
0.6M NaCl in 0.05M potassium phosphate, 1 mM EDTA and 1 mM
NaN3 of pH 7.0 to remove salt soluble protein, followed by a deion-
ized water wash 6 times, and freeze-dried. The freeze-dried proteins
were hand-powdered with a mortar and a pestle. The protein content
in each protein fraction was determined using the Kjeldahl nitrogen
procedure (AOAC, 1990). The powdered samples were stored at 4°C
and used within a week.
Sodium dodecyl sulphate - polyacrylamide gel
electrophoresis (SDS-PAGE)
The sarcoplasmic and myofibrillar fractions were subjected to SDS-
PAGE as described by Claeys et al. (1995), with modifications as
follows. The protein solutions (0.1%, w/v) were prepared by dissolv-
ing the samples in 10% SDS solution. The stacking gel was 4%, and
the resolving gel 12% acrylamide. Sodium 2-mercaptoethanesulfonate
was used in the loading buffer in place of 2-mercaptoethanol accord-
ing to the procedures described by Singh (1994). Proteins (25 µg)
were loaded into each sample slot. The molecular weights of the pro-
tein components were determined by comparison of their relative
mobilities and order of migration with those of protein molecular
weight standards (15,000 - 200,000 Dalton MW standards for SDS-
PAGE, GIBCO Life Technologies, Detroit, MI).
Thermal analysis
Powdered chicken breast meat was prepared by grinding 20 freeze-
dried chicken breast patties, using a mortar and a pestle. The pow-
dered sarcoplasmic, myofibrillar, and stromal proteins were prepared
as described. All samples were stored at 4°C before thermal analysis.
This was done to allow uniform sub-samples for subsequent analy-
ses, and was assumed to have negligible impact on the thermal prop-
erties (Lan et al., 1995).
For thermal analysis, samples were scanned in a differential scan-
ning calorimeter (Pyris I, Perkin-Elmer Corporation, Norwalk, CT),
calibrated with indium for heat flow, temperature, and enthalpy. Each
sample was prepared in an aluminum pan (Perkin-Elmer kit No. 219-
0062) with deionized water at a sample: water ratio of 1:2.5 (w/w),
hermetically sealed, and allowed to equilibrate at 4°C for 24h before
scanning. The heating rate of the DSC scans was 10°C/min over a
range of 10-100°C. Empty aluminum pans were used as the reference
and for baseline corrections. The cp (J/(g°C)) was calculated by (sam-
ple heat flow rate, J/s - baseline heat flow rate, J/s)/(sample mass, g ∞
heating rate, °C/s). The extrapolated onset temperature (To) and end
temperature (Te) of transformation, temperature of peak transition (Tp),
and enthalpy of transition (⌬H) were calculated by thermal analysis
software (Pyris Series Thermal Analysis System, 1996).
Statistical analysis
Total weight per patty, moisture content, total protein content, total
lipid content, and the protein concentration in each fraction were deter-
mined for 20 replicate patties. Means and standard deviations of To,
Te, Tp, and ⌬H were determined by analyzing 6 replicate patties.
Specific heat data were calculated by averaging DSC scans for 6
replicates of each material.
RESULTS & DISCUSSION
Compositional analysis
The compositional data for the patties (Table 1) were compared
with published data. These values were generally consistent with a
report that myofibrillar, sarcoplasmic, and stromal proteins comprised
~56.2, 42.3, and 1.5% of the total chicken breast muscle protein,
respectively (Lan et al., 1995). Additionally, Lawrie (1979) reported
that myofibrillar and sarcoplasmic proteins comprised ~60 and 30%
of the total muscle protein, respectively. Differences of our values
from previous reports were likely due to the sources of the samples.
We used SDS-PAGE to evaluate the efficiency of extraction for the
protein fractions. The protein bands obtained from SDS-PAGE were
compared with appropriate standards and published data. The electro-
phoretic patterns of myofibrillar proteins showed two major bands as
myosin heavy chain and actin at 200K and 45K, respectively, and the
Table 1–Composition of chicken breast patties
Property Meana Std. dev.
Total mass, g 52.65 1.73
Total moisture content, % wet basis 78.55 3.57
Total protein, % dry basis 95.14 3.61
Total lipids, % dry basis 0.15 0.07
Myofibrillar, % of total protein 62.63 3.30
Sarcoplasmic, % of total protein 35.71 1.88
Stromal, % of total protein 1.66 0.56
an=20; carbohydrates and ash comprised less than 5% of the dry mass
electrophoretic patterns of sarcoplasmic proteins were similar to those
reported by Hay et al. (1973). This indicated that the separation meth-
odologies were effective, resulting in the appropriate, distinct protein
fractions.
Thermal denaturation
The onset (To), end (Te), and peak (Tp) temperatures of protein
denaturation were evaluated for the chicken breast patties and their
protein constituents (Table 2). The enthalpies of protein denaturation
were also evaluated for sarcoplasmic, myofibrillar and stromal pro-
teins, and chicken breast patties (Table 3). For convenience of com-
parison, an identification number (1 to 6) was arbitrarily assigned to
each integral transition for the protein constituents and then applied to
the corresponding transitions for the breast patties.
For sarcoplasmic proteins, three transitions (no. 4, 5, and 6) were
observed, with Tp’s of 64.2, 71.9, and 78.4°C, respectively (Table 2).
The results by Kijowski and Mast (1988b) exhibited 3 peaks for
sarcoplasmic proteins at a temperature range of 60 - 80°C. Wang and
Smith (1994) reported that the DSC endotherm of sarcoplasmic pro-
teins of chicken breast muscle exhibited 3 peaks at 62, 67, and 72°C.
Although our mean values differed from the published values, consid-
ering differences in sample sources, our results were generally con-
sistent with previous data.
The myofibrillar proteins exhibited two transitions (no. 1 and 2),
with (⌬H’s of 0.4 and 0.3 J/(g°C), respectively (Table 2). Of the
myofibrillar proteins, myosin and actin are the two major components
(Judge et al., 1989). A comparable ⌬HH of 0.3 J/g was reported by
Xiong et al. (1987) for chicken actin, prepared from thigh muscle of 4
broilers.
The influence of pH and ionic strength on the Tp of myofibrillar
protein has been well documented (Ma and Harwalkar, 1991; Staburs-
vik and Marten, 1980; Goodno and Swenson, 1975; Wright et al.,
1977). Kijowski and Mast (1988a, b), in their detailed studies, indi-
cated that the thermal denaturation of isolated myofibrillar proteins
might yield 1, 2, or 3 transitions, and the number and temperature of
transitions were dependent upon pH and ionic strength. Our study
was conducted at a neutral pH and an ionic strength near zero. The two
Tp’s of myofibrillar proteins were 35.0 and 54.1°C, respectively.
One transition (no. 3) was observed for the stromal proteins at a Tp
of 64.2°C (Table 2). Stromal proteins constitute collagen and associ-
ated insoluble proteins. Xiong et al. (1987), and Kijowski and Mast
(1988a), in analysis of chicken breast muscle, reported that collagen
appeared as a single thermal denaturation peak at ~63 and 65.3°C,
respectively. Lan et al. (1995) suggested that collagen was the pre-
dominant stromal protein in chicken breast muscle. Consequently, our
denaturation temperature of the stromal protein agreed fairly well with
that of collagen reported by Xiong et al. (1987) , and Kijowski and
Mast (1988a). The ⌬H for the stromal proteins (no. 3) was the smallest
enthalpy of transition among the tested protein fractions (see Table 3).
Kijowski and Mast (1988a) studied chicken breast muscle from 7-
wk-old chicken broilers and obtained 5 endothermic peaks at 57, 62,
67, 72, and 79°C. We used ground and formed chicken breast patties
and observed 3 transitions at 52-57, 67-72, and 76-83°C. The differ-
ence in numbers of peaks from the previous report could be due to the
source of raw materials. Significant differences in physicochemical
and functional properties among the type, age, sex, and storage of
chicken meat were reported by Xiong and Brekke (1989).
Volume 63, No. 1, 1998— JOURNAL OF FOOD SCIENCE— 89
Specific Heat of Chicken Proteins . . .
Table 2–Transformation temperatures of chicken breast patties and their constituent proteinsa
Peak Chicken breast muscle Sarcoplasmic proteins Myofibrillar proteins Stromal proteins
no. (°C) (°C) (°C) (°C)
To Te Tp To Te Tp To Te Tp To Te Tp
1 31.76 37.86 34.99
(2.17) (0.46) (1.45)
2 52.29 56.67 52.90 50.88 58.44 54.14
(2.48) (1.84) (2.21) (0.82) (0.92) (0.45)
3 59.61 68.37 64.18
(0.45) (1.44) (0.54)
4 58.70 67.11 64.22
(0.77) (0.19) (0.35)
5 67.04 72.44 69.76 67.68 76.06 71.93
(0.8) (1.29) (0.74) (0.17) (0.92) (0.09)
6 76.31 82.84 78.91 77.22 82.84 78.45
(1.56) (1.79) (2.43) (1.75) (4.52) (1.76)

aValues reported are means (n=6), with standard deviations given in parentheses. T , T , and T are onset, end, and peak temperature, respectively, for each of the six different observed
o e p
transitions.

Table 3–Enthalpy of denaturation (⌬H) of chicken breast patties and
their constituent proteinsa
No Chicken breast Scaroplasmic Myofibrillar
muscle proteins proteins
(J/g) (J/g) (J/g)
1 0.44 (0.25)
2 0.19 (0.12) 0.33 (0.02)
3 0.18 (0.08)
4 0.21 (0.02)
5 0.90 (0.30) 2.50 (0.30)
6 0.11 (0.04) 0.29 (0.19)
aValues reported are means (n=6), with standard deviations given in parentheses.
The enthalpies of denaturation for the patty meat were also com-
pared to the endotherms for the constituent proteins. ⌬H no. 2 for the
patty (Table 3) was ~60% of the magnitude of ⌬H no. 2 for the
myofibrillar proteins. Also, ⌬H’s no. 5 and 6 for the patties were ~36
and 37% of ⌬H’s nos. 5 and 6 for sarcoplasmic proteins, respectively.
These results agreed well with the compositional analysis for the
myofibrillar and sarcoplasmic proteins (Table 1). The DSC scans of
chicken breast patties did not reflect transition no. 1 (from the myo-
fibrillar proteins), transition no. 3 (from stromal proteins), or transi-
tion no. 4 (from the sarcoplasmic proteins). This may have been due to
Fig. 1—Mean (n=6) apparent specific heats (Cp) of sarcoplasmic, myo-
fibrillar, and stromal proteins, and chicken breast patties as related
to temperature over a temperature range of 10–100°C (n=6). The
additive specific heat (dotted line) is equal to 0.3571 ∞ (specific heat
of sarcoplasmic protein) + 0.6263 ∞ (specific heat of myofibrillar
protein) + 0.166 ∞ (specific heat of stromal protein). The arrows mark
the endothermic peaks, as identified in Tables 2 and 3.
the protein-protein/solid interactions within the chicken breast patties.
Additionally, these peaks exhibited relatively small ⌬H’s, which might
Stromal not have been discernible in the scans of the patties.
proteins
Our preliminary results indicate that although the patty meat was
inherently complex, it yielded characteristic thermograms, which might
be interpreted in terms of the thermal denaturation of the individual
protein components. The DSC transitions found in the chicken breast
patties were assigned to myofibrillar and sarcoplasmic proteins. Be-
cause of the low content of the stromal proteins in the patties, the DSC
transition of the stromal proteins (64.2°C) was not observed in the
DSC scan of chicken breast patty. However, the contribution of stro-
mal proteins to overall muscle properties should not be overlooked.
The possibility that some of the thermal transitions were reversible
was investigated by re-scanning samples over the same temperature
range. In all cases, no transitions were observed in the re-scanned
samples, indicating that under these conditions the denaturation was
irreversible.
Specific heat
The mean apparent cp’s from 6 DSC scans of sarcoplasmic pro-
teins, myofibrillar proteins, stromal proteins, and chicken breast pat-
ties were compared (Fig. 1). Also the additive cp (dotted line), was
calculated as a weighted average cp of each protein component, based
on the weight fractions (Table 1). Although a slight deviation (±0.035
at the maximum) was observed at transitions between 60-80°C, the
calculated cp agreed well with the experimental data for the chicken
breast patties.
This slight deviation was possibly due to the protein-protein inter-
actions in the muscle meat complex. Changes in protein denaturation
induced by protein-protein interaction have been reported by Dono-
van and Beardslee (1975), Ledward (1978), Acton and Dick (1986),
and Xiong and Brekke (1990). In our results, the interaction between
protein and other solids was not a concern, given the low concentra-
tion of non-protein component in the patties. Based on the observation
that only minor conformational changes occurred during complex
formation, Ma and Harwalkar (1991) indicated that the effect of pro-
tein-protein interaction was due to kinetic, rather than thermodynamic
factors. Their observation was supported by our findings in this paper
that the enthalpies of the chicken breast patty were additive from the
enthalpies of the contributing constituents. Furthermore, because of
the relatively low values of the enthalpy changes (Table 3), this devi-
ation of calculated from experimental data would be negligible for the
target application of process simulation.
Temperature effect
Temperature affected the apparent cp’s of individual protein differ-
ently. The specific heats of sarcoplasmic and myofibrillar proteins
increased ~34 and 29%, respectively, with increasing temperature from
10 to 100°C. The specific heat of chicken breast patties also increased

90—JOURNAL OF FOOD SCIENCE—Volume 63, No. 1, 1998

with temperature. However, little temperature effect was observed for
the cp’s of stromal proteins. These changes in cp’s of the sarcoplasmic
protein, myofibrillar protein, stromal protein, and chicken breast meat
may be attributed to changes in the protein structures upon heating.
CONCLUSIONS
FOR GROUND BREAST MEAT, BOTH COMPOSITION AND TEMPERATURE
affected cp’s of chicken breast patties. Additionally, the endothermic
transitions in chicken breast patties corresponded to the denaturation
of their constituent proteins. This information can provide fundamen-
tal data required for developing thermal processing models for com-
mercial poultry products. By knowing the composition, the specific
heat of various poultry products might be predicted from the cp’s of
individual constituents, and the time-temperature history.
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Arkansas Agricultural Experiment Station Manuscript No. 97038.
This research was partially supported by the USDA NRI Competitive Grants Program, award No. 96-
35500-3550. The chicken patties used in the project were graciously provided by Tyson Foods,
Springdale, AR.
Volume 63, No. 1, 1998— JOURNAL OF FOOD SCIENCE— 91