期刊
INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
卷 43, 期 12, 页码 2143-2150出版社
WILEY-BLACKWELL
DOI: 10.1111/j.1365-2621.2008.01821.x
关键词
Casein; matrix metalloprotease-13; protein aggregation; sarcoplasm; small heat shock protein; alpha A-crystallin; alpha B-crystallin; mu-calpain
资金
- Foundation for Research Science and Technology (New Zealand) programme 'Foods that Delight' [C10X0201]
The ability of small heat shock proteins (sHSP) at preventing the aggregation and precipitation of unfolded and misfolded proteins because of changes in pH and temperature is widely recognised. The performance of sHSP from bovine lens extract at protecting sarcoplasmic proteins from heat induced denaturation and aggregation was compared with other chaperones including bovine serum albumin, alpha(s)-casein, beta-casein and a synthetic peptide based upon alpha A-crystallin (AAC). Beef sarcoplasmic proteins were heated in the presence or absence of exogenous chaperone and the solubility, surface hydrophobicity and enzymatic activities of the sarcoplasmic proteins was determined. Lens extract prevented the aggregation of sarcoplasmic proteins, maintaining solubility and clarity up to 65 degrees C relative to 60 degrees C for beta-casein. By contrast, alpha(s)- and beta-casein proteins protected the activity of endogenous enzymes at temperatures between 37 degrees C and 52 degrees C, unlike lens sHSP. Our findings support the addition of casein proteins as potential thermal stabilisers of meat proteins in food systems.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据