期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 50, 期 6, 页码 1569-1573出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf010763l
关键词
soy protein isolate; gelation; rheology; rearrangements; protein-protein interactions
Heat-induced gel formation by soy protein isolate at pH 7 is discussed. Different heating and cooling rates, heating times, and heating temperatures were used to elucidate the various processes that occur and to study the relative role of covalent and noncovalent protein interactions therein. Gel formation was followed by dynamic rheological measurements. Heat denaturation was a prerequisite for gel formation. The,gelation temperature (84 degreesC) was just above the onset denaturation temperature of glycinin. The stiffness of the gels, measured as the elastic modulus, G, increased with the proportion of denatured protein. An increase in G' was also observed during prolonged heating at 90 degreesC. This increase is explained by the occurrence of rearrangements in the network structure and probably also by further incorporation of protein in the network. The increase in 9 upon cooling was thermoreversible indicating that disulfide bond formation and rearrangements do not occur upon cooling.
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