Effects of Thermal Treatment of Soy Protein Isolate on the Characteristics and Structure-Function Relationship of Soluble and Insoluble Fractions

Autor:	María Cristina Añón, Delia A. Sorgentini, Jorge R. Wagner
Rok vydání:	1995
Předmět:	Chromatography Chemistry Structure function Molar mass distribution Denaturation (biochemistry) Fraction (chemistry) General Chemistry Thermal treatment Solubility General Agricultural and Biological Sciences Soy protein Degree (temperature)
Zdroj:	Journal of Agricultural and Food Chemistry. 43:2471-2479
ISSN:	1520-5118 0021-8561
DOI:	10.1021/jf00057a029
Popis:	Aqueous dispersions (5-15% w/w) of native soy protein isolate were thermally treated at 80 and 100 °C for 30 min. At 100 °C, both 7S and 11S proteins were totally denatured, while at 80 °C, the 7S protein-was totally denatured but the 11S protein was not, the denaturation degree of which was only partial and dependent on the extent of isolate denaturation. The different behaviors were reflected in the degree of aggregation, which in turn determined the yields and structural characteristics (denaturation degree, molecular weight distribution, superficial hydrophobicity, Mg 2+ induced aggregation) of soluble and insoluble fraction obtained from treated isolates. A study was then performed on the effects of such structural changes on some functional properties (solubility, water imbibing, gelling and foaming properties) of soluble and insoluble fractions and, consequently, those of the total isolate.
Databáze:	OpenAIRE
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