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

Abstract

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

TANG Chuan-He, YANG Xiao-Quan, CHEN Zhong, PENG Zhi-Ying. Study on Catalytic Characteristics and Mechanism of Microbial Transglutaminase (MTGase)Polymerization of Protein Substrates——(I) Catalytic Charactertistics of MTGase against Mono-substrate Proteins[J]. FOOD SCIENCE, 2003, 24(5): 19-24.

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

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