期刊
FOOD HYDROCOLLOIDS
卷 22, 期 5, 页码 752-762出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2007.03.003
关键词
beta-lactoalobulin; dextran sulfate; thermal stability; NaCl; SEC-MALLS; aggregation
The effects of NaCl, dextran sulfate (DS), and initial protein concentration on thermal stability of beta-lactoglobulin (beta-LG) and alpha-lactalbumin (alpha-LA) at pH 6.8 were investigated. NaCl was the biggest factor in accelerating protein aggregation as shown by an increase in turbidity. molecular size, and a decrease in protein solubility. DS at low concentration showed a protective effect against aggregation. Evidence suggested some degree of interaction between beta-LG and DS. At higher concentration, phase separation between biopolymers favored aggregation, which resulted in an increase in turbidity and a reduction in protein solubility. (c) 2007 Elsevier Ltd. All rights reserved.
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