Caseins: Utilizing Molecular Chaperone Properties to Control Protein Aggregation in Foods
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 58(2), 685–693.
By:
Y. Yong n & E. Forgeding
author keywords: beta-Casein; alpha(s)-casein; molecular chaperone; intrinsically unstructured protein
MeSH headings : Animals; Caseins / chemistry; Cattle; Chickens; Food Technology; Milk Proteins / chemistry; Molecular Chaperones / chemistry; Protein Folding; Proteins / chemistry; Whey Proteins
TL;DR:
While it is clear that caseins can alter aggregation at neutral pH, their effectiveness at low pH, high protein concentration, and high thermal treatment remains to be fully established.
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