Apparent Specific Heat of Chicken Breast Patties and their Constituent Proteins by Differential Scanning Calorimetry

Abstract

Chicken breast meat yielded three endothermic transitions, with peak transition temperatures of 53,70, and 79°C. Comparison with the purified protein fractions indicated that these transitions corresponded to denaturation of myofibrillar (53°C) and sarcoplasmic (70 and 79°C) proteins. The apparent specific heat profile of chicken breast meat was successfully 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; however, the specific heat of stromal protein was nearly constant across the temperature range considered (i.e., 10 to 100°C).

Cryoprotective effect of trehalose on washed chicken meat

“…Denaturation temperatures (T p ) of myosin and actin for WCM with trehalose (w=0-10%) at 0, 30, 90, 180 and 360 day of frozen storage are presented in Table 1. Values of denaturation temperatures (T p ) of myosin and actin were different then values of raw chicken breast meat reported by Kijowski and Mast (1988), Murphy et al (1998) and Bircan and Barringer (2002). Similar results was reported by Kijowski and Richardson (1996) for washed mechanically deboned poultry meat, this could be explained by concentration of myofibrillar protein by washing and different pH and ionic environment when compared to the raw state of muscle (Wright and Wilding 1984;Xiong et al 1987;Lesiow and Xiong 2001).…”

Antioxidative Ability of Chicken Myofibrillar Protein Developed by Glycosylation and Changes in the Solubility and Thermal Stability

“…The thermal stability was followed by monitoring the change in solubility of the protein solution during heating according to a modification to the method of Fujiwara et al 14) Murphy et al 25) have reported by differential scanning calorimetry that chicken myofibrillar protein was thermally denatured at 53 C, so 50 C was used as the incubation temperature in order to examine the effect on solubility of this denaturation temperature. Lyophilized myofibrillar proteins mixed with maltose at a weight ratio of 1:4 were kept at 60 C and 35% RH for 24 or 36 h. After incubating for glycosylation, the protein powder was immediately mixed with 0.1 or 0.5 M NaCl-40 mM Tris-malate (pH 7.5) at 2 mg/mL of final protein concentration with an Ultra-turrax T25-S1 high-speed blender (IKA-Labotechnik, Staufen, Germany) twice at 10,000 rpm for 0.5 min each (1 min total) and then dialyzed against the same NaCl solution at 4 C for 16 h. The unreacted maltose was removed in this step.…”

Effect of marination on the thermodynamic properties of chicken muscle proteins studied by DSC

“…On the thermal curve, three endothermic transitions are visible, which can be ascribed to the denaturation temperatures (T max ) of myosin (51°C), sarcoplasmic and connective tissue proteins (56°C), and actin (68°C). Typical transition temperatures of chicken breast muscle (pectoralis major) can range from 49°C to 57°C for myosin and its subunits, 61-67°C for sarcoplasmic proteins, and 76-79°C for actin (Xiong et al 1987;Kijowski & Mast 1988;Wang & Smith 1994;Murphy et al 1998;Wattanachant et al 2005;Bertram et al 2006). On the basis of the collected results (Table 2), it may be stated that the values of enthalpy and denaturation temperature in all marinated samples differed significantly (P < 0.05) from the non-marinated sample, for which the highest values of enthalpy and denaturation temperatures of myosin and actin were recorded.…”