微生物转谷氨酰胺酶对酪蛋白酸钠的交联作用。

Die Nahrung Pub Date : 1998-08-01 DOI:10.1002/(sici)1521-3803(199808)42:03/04<151::aid-food151>3.3.co;2-5

P C Lorenzen, E Schlimme, N Roos

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引用次数: 57

摘要

酪蛋白酸钠是谷氨酰胺转胺酶的有效底物。交联反应速度快，交联程度高。该聚合物可被胰蛋白酶水解，但蛋白水解产物含有未水解或部分水解的聚集体的残留部分。水解酪蛋白酸钠的交联减少了游离氨基的数量，但只导致肽分子量的非常小的增加。

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Crosslinking of sodium caseinate by a microbial transglutaminase.

Sodium caseinate is an effective substrate for transglutaminase. Crosslinking takes place at fast reaction rates resulting in high degrees of crosslinking. The polymers can be hydrolysed by trypsin, but the proteolysates contain residual portions of non- or partlyhydrolysed aggregates. Crosslinking of hydrolysed sodium caseinate decreased the number of free amino groups, but leads only to a very small increase in molecular weight of the peptides.

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Die Nahrung

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