Kuipers Bas J H, Alting Arno C, Gruppen Harry
Department of Agrotechnology and Food Sciences, Laboratory of Food Chemistry, Wageningen University, P.O. Box 8129, 6700 EV Wageningen, The Netherlands.
Biotechnol Adv. 2007 Nov-Dec;25(6):606-10. doi: 10.1016/j.biotechadv.2007.07.005. Epub 2007 Aug 2.
Soy-derived proteins (soy protein isolate, glycinin, and beta-conglycinin) and bovine whey-derived proteins (whey protein isolate, alpha-lactalbumin, beta-lactoglobulin) were hydrolyzed using subtilisin Carlsberg, chymotrypsin, trypsin, bromelain, and papain. The (in)solubility of the hydrolysates obtained was studied as a function of pH. At neutral pH, all soy-derived protein hydrolysates, particularly those from glycinin, obtained by hydrolysis with subtilisin Carlsberg, chymotrypsin, bromelain, and papain showed a stronger aggregation compared to the non-hydrolyzed ones. This increase in aggregation was not observed upon hydrolysis by trypsin. None of the whey-derived protein hydrolysates exhibited an increase in aggregation at neutral pH. The high abundance of theoretical cleavage sites in the hydrophobic regions of glycinin probably explains the stronger exposure of hydrophobic groups than for the other proteins, which is suggested to be the driving force in the aggregate formation.
大豆衍生蛋白（大豆分离蛋白、大豆球蛋白和β-伴大豆球蛋白）和牛乳清衍生蛋白（乳清分离蛋白、α-乳白蛋白、β-乳球蛋白）使用枯草杆菌蛋白酶、胰凝乳蛋白酶、胰蛋白酶、菠萝蛋白酶和木瓜蛋白酶进行水解。研究了所得水解产物的（不）溶性与pH值的关系。在中性pH条件下，所有大豆衍生蛋白水解产物，特别是通过枯草杆菌蛋白酶、胰凝乳蛋白酶、菠萝蛋白酶和木瓜蛋白酶水解大豆球蛋白得到的水解产物，与未水解的产物相比，表现出更强的聚集性。胰蛋白酶水解时未观察到聚集性增加。在中性pH条件下，没有一种乳清衍生蛋白水解产物表现出聚集性增加。大豆球蛋白疏水区域中理论切割位点的高丰度可能解释了与其他蛋白质相比，疏水基团的暴露更强，这被认为是聚集体形成的驱动力。
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