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Thermal Aggregation of Soybean (Glycine max L.) Sulfur‐rich Protein
Author(s) -
SATHE S. K.,
MASON A. C.,
WEAVER C. M.
Publication year - 1989
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1989.tb03071.x
Subject(s) - chemistry , hydrogen bond , protein aggregation , salt (chemistry) , hofmeister series , sulfur , glycine , hydrophobic effect , disulfide bond , chromatography , amino acid , organic chemistry , biochemistry , molecule
The sulfur‐rich protein (SRP) in soybeans aggregated at ≥ 70°C due to thermal denaturation of the protein and subsequent formation of soluble and insoluble aggregates. Aggregation was dependent on heating temperature, time, buffer composition, and the presence or absence of protein modifying agents in the heating buffer. Hydrophobic interactions and disulfide bonds helped stabilize the protein against thermal aggregation while hydrogen bonds and sulfhydryl exchange promoted it. At pH 7.6, 4.5 mg protein/mL, 70°C and 1.0M salt concentration, the rate of thermal aggregation was dependent on the anion type and followed lyotropic series SCN‐> I‐> Br‐> Cl −