Characterization of Glutamate Decarboxylase from Lactobacillus plantarum and Its C-Terminal Function for the pH Dependence of Activity

被引：50

作者：

Shin, Sun-Mi ^{[1
]}

Kim, Hana ^{[2
]}

Joo, Yunhye ^{[1
]}

Lee, Sang-Jae ^{[3
]}

Lee, Yong-Jik ^{[1
]}

Lee, Sang Jun ^{[4
]}

Lee, Dong-Woo ^{[1
]}

机构：

[1] Kyungpook Natl Univ, Sch Appl Biosci, Taegu 702701, South Korea

[2] SAMSUNG BIOEPIS Corp, Inchon 406840, South Korea

[3] Silla Univ, Dept Biofood Mat, Pusan 617736, South Korea

[4] KRIBB, Infect & Immun Res Ctr, Taejon 305806, South Korea

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2014年 / 62卷 / 50期

基金：

新加坡国家研究基金会;

关键词：

pH dependence; glutamate decarboxylase; C-terminal region; GABA; Lactobacillus plantarum; GAMMA-AMINOBUTYRIC-ACID; ESCHERICHIA-COLI; LISTERIA-MONOCYTOGENES; LACTOCOCCUS-LACTIS; RESISTANCE; GABA; PURIFICATION; TOLERANCE; SYSTEM; EXPRESSION;

D O I：

10.1021/jf504656h

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

The gadB gene encoding glutamate decarboxylase (GAD) from Lactobacillus plantarum was cloned and expressed in Escherichia coli. The recombinant enzyme exhibited maximal activity at 40 degrees C and pH 5.0. The 3D model structure of L. plantarum GAD proposed that its C-terminal region (Ile454-Thr468) may play an important role in the pH dependence of catalysis. Accordingly, C-terminally truncated (Delta 3 and Delta 11 residues) mutants were generated and their enzyme activities compared with that of the wild-type enzyme at different pH values. Unlike the wild-type GAD, the mutants showed pronounced catalytic activity in a broad pH range of 4.0-8.0, suggesting that the C-terminal region is involved in the pH dependence of GAD activity. Therefore, this study may provide effective target regions for engineering pH dependence of GAD activity, thereby meeting industrial demands for the production of gamma-aminobutyrate in a broad range of pH values.

引用

页码：12186 / 12193

页数：8

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