Affiliation:
1. The Ohio State University, Columbus, Ohio 43210; The Ohio Agricultural Research and Development Center, Wooster, Ohio 44691s2; and Catedra de Tecnologia y Bioquimica de los Alimentos, Facultad de Veterinaria, Cordoba, Spain
Abstract
Sarcoplasmic, myofibrillar, and non-protein nitrogen fractions extracted from chicken leg and breast muscle tissue after heating to 40, 50, 60, 70, and 80 C were compared with non-heated samples. The pH modifications that occurred during heating were also observed. The myofibrillar fraction was more heat-sensitive than the sarcoplasmic proteins with a slight difference in sensitivity occurring between the leg and breast muscle tissues. Both of these fractions were only approximately 10% soluble after heating to 70 C with only slight alterations caused by additional heating to 80 C. The non-protein nitrogen fractions decreased slightly during the heating cycle and remained more than 90% soluble after heating to 80 C. Initially, pH of breast muscle was lower (P < .05) than leg muscle and the breast sample increased in pH more rapidly than the leg sample during the heating cycle.
Publisher
International Association for Food Protection
Subject
Microbiology,Food Science
Cited by
10 articles.
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