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| Effects of glycosylation and trypsin enzymolysis on conformation and functional properties of soybean protein |
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| KeyWord:soybean protein isolate glycosylation trypsin hydrolysis tertiary structure functional property |
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| Abstract: |
| The glycosylated soybean protein (GSPI) was first generated from soybean protein isolate (SPI) and oligochitosan catalyzed by transglutaminase and then hydrolyzed by trypsin to prepare hydrolysates with hydrolysis degrees (DH) of 1%, 5%, 10% and 15%. The effects of glysosylation and enzymolysis on the tertiary structure and functional properties of SPI were investigated. The results showed that GSPI and its hydrolysates had more loosen tertiary structure than SPI. The thermal stabilities of GSPI hydrolysates(DH 15%) after thermal treatment (85?℃)were 50.74% at pH 4.0 and 67.66% at pH 7.0, respectively, indicating that thermal stabilities of GSPI hydrolysates were better. GSPI showed an increasing foam stability, and its trypsin hydrolysates with DH 10% exhibited the highest foamability. GSPI also showed an increased emulsion stability, and its trypsin hydrolysates with DH 5% exhibited better emulsion stability. The modified SPI showed different in vitro digestibilities. GSPI was less sensitive to pepsin hydrolysis, while its hydrolysates were less sensitive to trypsin hydrolysis. |
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