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Solubility and Emulsifying Properties of Soy Protein Isolates Modified by Pancreatin

机译:胰酶修饰的大豆分离蛋白的溶解性和乳化特性

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Soy protein isolates (SPI) with varying degrees of hydrolysis (DH of 7, 11, 15, 17/100) were produced using pancreatin. The surface hydrophobiclty indices of pancreatin hydrolyzed SPI (PSPI) (34.5, 34.9, 39. 1, and 40.7 for 7, 11, 15, 17/100 DH, re- spectively) were higher than that of SPI (10.5) and control SPI (CSPI) (12.5, 11.9, 12.9, and 12.6 for 10, 60, 120, and 180 rain incubation, respectively). The solubilities of PSPI at pH 4.5 were 2.7, 9.1, 11.9, and 18.7/100, for 7, 11, 15, and 17/100 DH, respectively, while the solubilities of SPI and CSPI at the same pH were about 1.6/100. Solubilities of PSPI at pH 7.0 were > 90/100 for all DHs tested, while those of SPI and CSPI were 85/100. The emulsifying activity index (EAI) of PSPI increased with increasing DH. PSPI with 15/100 DH had highest EAI (1. 122) which was higher (P < 0. 05) than those of SPI (0.550) and CSPI after 120 rain incubation without enzyme (0.568). These results suggest that PSPI could be used as an ingre- dient for emulsified products and where high solubility at low pH is required.
机译:使用胰酶生产具有不同水解度(DH为7、11、15、17 / 100)的大豆分离蛋白(SPI)。胰酶水解SPI(PSPI)的表面疏水指数(分别为7、11、15、17 / 100 DH的34.5、34.9、39.1,和40.7)高于SPI(10.5)和对照SPI的表面疏水指数(CSPI)(对于10、60、120和180的雨水培养分别为12.5、11.9、12.9和12.6)。对于4.5、7、11、15和17/100 DH,PSPI在pH 4.5下的溶解度分别为2.7、9.1、11.9和18.7 / 100,而在相同pH下SPI和CSPI的溶解度约为1.6 / 100 。对于所有测试的DH,在pH 7.0下PSPI的溶解度均> 90/100,而SPI和CSPI的溶解度则为85/100。 PDH的乳化活性指数(EAI)随DH的增加而增加。在没有酶的条件下进行120次雨水培养后,具有15/100 DH的PSPI的EAI最高(1.122),高于(P <0。05)(0.550)和SPI(0.568)。这些结果表明,PSPI可以用作乳化产品的成分,并且要求在低pH下具有高溶解度。

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