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Molecular Bases of Surface Activity of Proteins

机译:蛋白质表面活性的分子基础

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The first critical event in the creation of protein-stabilized emulsions and foams is adsorption of proteins at the oil-water and air-water interfaces. This initial event is dependent on the molecular flexibility of proteins. The dynamic equation-of-state, #THETA#, of proteins at the air-water and oil-water interfaces is directly related to flexibility. The #THETA# value of proteins, which represents dynamic reduction in interfacia free energy per mg of adsorbed protein (ergs/mg), at the air-water interface is also linearly correlated with the emulsifying properties, foaming properties, proteolytic digestibility, and the adiabatic compressibility of proteins. Based on these correlations, it is proposed that the #THETA# values of proteins can be used as a predictor of several functional properties of proteins.
机译:产生蛋白质稳定的乳液和泡沫的第一个关键事件是蛋白质在油-水和空气-水界面处的吸附。此初始事件取决于蛋白质的分子柔性。空气-水和油-水界面处的蛋白质动态状态方程#THETA#与柔韧性直接相关。蛋白质的#THETA#值表示在空气-水界面处每毫克吸附的蛋白质的界面自由能的动态降低(ergs / mg)也与乳化特性,起泡特性,蛋白水解消化率和蛋白质的绝热可压缩性。基于这些相关性,建议蛋白质的#THETA#值可用作蛋白质几种功能特性的预测指标。

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