APPARENT SPECIFIC-HEAT OF CHICKEN BREAST PATTIES AND THEIR CONSTITUENT PROTEINS BY DIFFERENTIAL SCANNING CALORIMETRY

Citation
Ry. Murphy et al., APPARENT SPECIFIC-HEAT OF CHICKEN BREAST PATTIES AND THEIR CONSTITUENT PROTEINS BY DIFFERENTIAL SCANNING CALORIMETRY, Journal of food science, 63(1), 1998, pp. 88-91
Citations number
47
Categorie Soggetti
Food Science & Tenology
Journal title
ISSN journal
00221147
Volume
63
Issue
1
Year of publication
1998
Pages
88 - 91
Database
ISI
SICI code
0022-1147(1998)63:1<88:ASOCBP>2.0.ZU;2-M
Abstract
Chicken breast meat yielded three endothermic transitions, with peak t ransition temperatures of 53, 70, and 79 degrees C. Comparison with th e purified protein fractions indicated that these transitions correspo nded to denaturation of myofibrillar (53 degrees C) and sarcoplasmic ( 70 and 79 degrees C) proteins. The apparent specific heat profile of c hicken breast meat was successfully modeled as a weighted average of t he apparent specific heat of the constituent proteins. The specific he ats of sarcoplasmic protein, myofibrillar protein, and chicken breast meat were strongly influenced by temperature; however, the specific he at of stromal protein was nearly constant across the temperature range considered (i.e., in to 100 degrees C).