Nötzold H, Winkler H, Wiedemann B, Ludwig E
Nahrung. 1984;28(3):299-308. doi: 10.1002/food.19840280322.
Lysinoalanine (LAL) was determined in alkali-treated partial hydrolysates (PH) of casein, peptides isolated from these PH and in PH of field-bean protein to clarify whether intermolecular or intramolecular LAL bridges are preferentially formed. Furthermore, the formation of LAS in plasteins was studied as a contribution to plastein research. The formation of LAL in the peptide mixtures of beta-casein and the decrease of the LAL content in the PH (as compared to intact proteins) indicates that the formation of LAL favours the intramolecular cross-linking of polypeptide chains. The LAL content decreases as the degree of hydrolysis of the PH of the field-bean protein isolate increases, and depends upon the protease used in the production of the hydrolysates. The LAL contents of the alkali-treated plasteins are less than those of the initial hydrolysates. The decrease of the LAL content is directly proportional to the hydrolysis proceeding during the plastein reaction.
测定了酪蛋白碱处理部分水解产物（PH）、从这些PH中分离出的肽以及蚕豆蛋白PH中的赖氨酰丙氨酸（LAL），以阐明分子间或分子内LAL桥是否优先形成。此外，还研究了塑性蛋白中LAL的形成，作为对塑性蛋白研究的一项贡献。β-酪蛋白肽混合物中LAL的形成以及PH中LAL含量的降低（与完整蛋白质相比）表明，LAL的形成有利于多肽链的分子内交联。蚕豆蛋白分离物PH的LAL含量随着水解程度的增加而降低，并取决于水解产物生产中使用的蛋白酶。碱处理塑性蛋白的LAL含量低于初始水解产物。LAL含量的降低与塑性蛋白反应过程中的水解程度成正比。
