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Surface properties and structure characteristics of soybean protein isolate by limited hydrolysis

机译:水解有限水解的大豆蛋白分离物的表面性质及结构特征

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The surface adsorption properties of soy protein isolated (SPI) were obviously improved after limited hydrolysis by trypsin. When the hydrolyzing degree (DH) of SPI was controlled from 2% to 6%, the surface tension behavior of modified SPI was decreased with the hydrolyzing degree increasing. Compared to the natural soy protein, the values of surface tension of modified SPI which DH was 4% decreased by 19.35% and the foamability increased by 22.03%. The variations of surface properties of modified SPI were related to its structural change, it presented better surface hydrophobic properties, lower electric surface charge, and the increased viscosity which was apt to adsorb at interface of two phase region as compared to the natural soy protein which had poor behaviors of foams and emulsions.
机译:在通过胰蛋白酶的有限水解后显然改善了大豆蛋白的表面吸附性能。 当SPI的水解度(DH)控制2%至6%时,随着水解度的增加,改性SPI的表面张力行为降低。 与天然大豆蛋白相比,DH为4%的改性SPI的表面张力值降低19.35%,发泡性增加22.03%。 改性SPI的表面性质的变化与其结构变化有关,它呈现出更好的表面疏水性质,较低的电容器电荷和增加的粘度,其与天然大豆蛋白相比,在两个相位区域的界面中易于吸附的粘度 泡沫和乳液的行为不佳。

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