食品科学 ›› 2003, Vol. 24 ›› Issue (5): 19-24.

• 基础研究 •    下一篇

微生物转谷氨酰胺酶(MTGase)的蛋白质底物催化特性及其催化机理研究 (I)MTGase催化单底物蛋白质的聚合特性

 唐传核, 杨晓泉, 陈中, 彭志英   

  1. 华南理工大学食品与生物工程学院
  • 出版日期:2003-05-15 发布日期:2011-12-13

Study on Catalytic Characteristics and Mechanism of Microbial Transglutaminase (MTGase)Polymerization of Protein Substrates——(I) Catalytic Charactertistics of MTGase against Mono-substrate Proteins

 TANG  Chuan-He, YANG  Xiao-Quan, CHEN  Zhong, PENG  Zhi-Ying   

  • Online:2003-05-15 Published:2011-12-13

摘要: 采用SDS-PAGE结合凝胶成像技术比较了MTGase在还原状态下对酪蛋白酸钠(SC)、牛血清蛋白(BSA)、大豆球蛋白(glycinin)和β-伴豆球蛋白(β-conglycinin)、β-乳球蛋白(β-LG)和α-乳白蛋白(α-LA)等单底物蛋白的聚合效率。结果表明MTGase较易催化SC和BSA聚合,其次为大豆球蛋白,而β-伴豆球蛋白、β-LG和α-LA最不易。根据MTGase催化不同单底物蛋白质的聚合速率的差异,对MTGase催化单底物蛋白质的聚合特性进行了探讨,指出:①底物蛋白的分子结构对MTGase催化活性的重要性;②蛋白质表面疏水度对MTGase催化活性的重要性;③对蛋白质进行一定的预处理可增强MTGase对蛋白质(特别是球蛋白)的催化活性。

关键词: 微生物转谷氨酰胺酶, 食物蛋白质, 聚合

Abstract: The polymerization of mono-substrate food proteins such as sodium caseinate, bovine serum albumin (BSA), glycininand β-conglycinin, β-lactoglobulin(β-LG) andα-lactoalbumin (α-LA) by MTGase were studied by SDS-PAGE combinedwith the technique of imaging. It showed that sodium caseinate and BSA were the best substrates of MTGase, and glycininfollowed next, andβ-conglycinin and whey proteins were poor substrates of MTGase. According to the differences of catalyticvelocity of MTGase towards different proteins, the polymerization characteristics of MTGase against mono-substrate proteinswere discussed. It was pointed out that, both the molecular structure of substrate protein and its surface hydrophobity (So) wereimportant for the catalytic activity of MTGase, and certain pretreatment of substrate proteins could improve the catalyticactivity of MTGase towards proteins (especially for globular proteins).

Key words: Microbial Transglutaminase(MTGase), food proteins, polymerization