作者: Catriona M. M. Lakemond , Harmen H. J. de Jongh , Martin Hessing , Harry Gruppen , Alphons G. J. Voragen
DOI: 10.1021/JF9908695
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摘要: This study describes the relationship between the solubility of glycinin, a major soy protein, and its structural properties at a quaternary, tertiary, and secondary folding level under conditions representative for food products. When the ionic strength is lowered from 0.5 to 0.2 or 0.03, the basic polypeptides shift more to the exterior of the glycinin complex, as determined at pH 7.6 by labeling solvent-exposed lysines, supported by the study of the proteolytic action of clostripain on glycinin. This structural reorganization caused the pH of …