期刊
JOURNAL OF FOOD SCIENCE
卷 65, 期 4, 页码 556-560出版社
INST FOOD TECHNOLOGISTS
DOI: 10.1111/j.1365-2621.2000.tb16047.x
关键词
fish myosin; aggregation; frozen stability; -SH groups; ATPase activity
Fish myosin obtained from Tilapia nilotica was solubilized in 20 mM Tris-HCl, pH 7.0, with 0.6 M KCl (solution model system), or suspended without salt (suspension model system). Changes in % soluble protein, Ca2+-ATPase activity, and total and reactive -SH groups during frozen storage were evaluated. Frozen induced aggregation of fish myosin showed different behavior depending upon its initial physicochemical state. When myosin was solubilized prior to frozen storage, head-to-head interactions seemed to be more involved in protein aggregation with a strong participation of disulfide bonds. On the contrary, a preferentially side-to-side mechanism might be involved in the aggregation of myosin upon suspension, with a minor interaction of -SH groups.
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