Transglutaminase from Streptoverticillium ladakanum and application to minced fish product

被引：46

作者：

Tsai, GJ ^{[1
]}

Lin, SM ^{[1
]}

Jiang, ST ^{[1
]}

机构：

[1] NATL TAIWAN OCEAN UNIV,DEPT MARINE FOOD SCI,CHILUNG 202,TAIWAN

来源：

JOURNAL OF FOOD SCIENCE | 1996年 / 61卷 / 06期

关键词：

microbial transglutaminase; mackerel surimi; Streptoverticillium ladakanum;

D O I：

10.1111/j.1365-2621.1996.tb10968.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The transglutaminase (TGase) from Streptoverticillium ladakanum was purified to electrophoretic homogeneity after ammonium sulfate fractionation and Blue Sepharose Fast Flow chromatography. The molecular weight of the purified TGase was 30.5 kDa estimated by Superdex 75HR gel filtration, and 37.5 kDa by SDS-PAGE. This enzyme, with optima at pH at 6.0 and 50 degrees C was very stable at pH 5.0 similar to 7.0. It was strongly inhibited by PCMB, PMSF, Pb2+, Zn2+ and Cu2+, but not affected by EDTA and Ca2+. This suggested that the purified TGase was calcium-independent and its active center contained cysteine. It catalyzed the crosslinking of fish myosin heavy chain and substantially increased the gel strength of mackerel surimi.

引用

页码：1234 / 1238

页数：5

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