Improved catalytic efficiency of a monomeric γ-glutamyl transpeptidase from Bacillus licheniformis in presence of subtilisin

被引：7

作者：

Tiwary, Ekta ^{[1
]}

Gupta, Rani ^{[1
]}

机构：

[1] Univ Delhi, Dept Microbiol, New Delhi 110021, India

来源：

BIOTECHNOLOGY LETTERS | 2010年 / 32卷 / 08期

关键词：

Bacillus licheniformis; gamma-glutamyl transpeptidase; GGT(30); GGT(30) + S; Subtilisin; PURIFICATION; IDENTIFICATION;

D O I：

10.1007/s10529-010-0271-3

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Monomeric 30 kDa gamma-glutamyl transpeptidase (GGT(30)) was purified from culture broth of Bacillus licheniformis ER-15 along with a heterodimeric 67 kDa GGT (GGT(67)). In presence of subtilisin, GGT(30) had improved catalytic efficiency (V-max/K-m) of 59 min(-1), altered pH and temperature optima of pH 11 and 70A degrees C.and had salt-tolerant glutaminase activity. Glutaminase activity was retained even in protease-inhibited condition in presence of 2 mM PMSF. GGT(30) and subtilisin complexation was also confirmed by relative electrophoretic mobility and fluorescence quenching experiment.

引用

页码：1137 / 1141

页数：5

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