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Surface Properties and Structure Characteristics of Soybean Protein Isolate by Limited Hydrolysis

机译:有限水解大豆分离蛋白的表面性质和结构特征

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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:胰蛋白酶限制水解后,大豆分离蛋白(SPI)的表面吸附性能明显提高。当将SPI的水解度(DH)控制在2%至6%时,改性SPI的表面张力行为随水解度的增加而降低。与天然大豆蛋白相比,DH为4%的改性SPI的表面张力降低了19.35%,发泡性提高了22.03%。改性SPI的表面性能变化与其结构变化有关,与天然大豆蛋白相比,具有更好的表面疏水性,较低的表面电荷和增加的粘度,易于在两相区域的界面吸附。泡沫和乳液的行为较差。

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