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Effects of ${\alpha}$-Chymotrypsin Modification on the Functional Properties of Soy Protein Isolates  

Ahn Tae-Hyun (National Institute of Crop Science, RDA)
Lee Sook-Young (Department of Food and Nutrition, Chung-Ang University)
Publication Information
KOREAN JOURNAL OF CROP SCIENCE / v.51, no.2, 2006 , pp. 148-153 More about this Journal
Abstract
Effects of ${\alpha}$-chymotrypsin modification on degree of hydrolysis (DH), solubility, emulsifying capacity and thermal aggregation of laboratory-purified soy protein isolate (SPI) using a lipoxygenase-defected soybean (Jinpum-kong) and commercial soy protein isolate (Supro 500E) were compared. SPIs were hydrolyzed by ${\alpha}$-chymotrypsin at pH 7.8 and $37^{\circ}C$ for 30 min. DHs of Supro 500E and Jinpum-kong SPI were increased by ${\alpha}$-chymotrypsin modification, and DH of Supro 500E was higher than that of Jinpum-kong SPI. DH of ${\alpha}$-chymotrypsin treated Jinpum-kong SPI was similar with untreated Supro 500E and DH of treated Supro 500E was the highest. Solubility, emulsifying capacity and thermal aggregation of SPIs were increased by ${\alpha}$-chymotrypsin modification, and these changes were highly related to changes in DH. Functional properties of Supro 500E were higher than Jinpum-kong SPI in both of untreated and ${\alpha}$-chymotrypsin treated SPIs.
Keywords
soy protein isolate; enzyme modification; solubility; emulsifying capacity; thermal aggregation;
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