Characterization of glutamate decarboxylase from Lactobacillus plantarum and its C-terminal function for the pH dependence of activity

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Title
Characterization of glutamate decarboxylase from Lactobacillus plantarum and its C-terminal function for the pH dependence of activity
Author(s)
S M Shin; H Kim; Y Joo; S J Lee; Y J Lee; Sang Jun Lee; D W Lee
Bibliographic Citation
Journal of Agricultural and Food Chemistry, vol. 62, no. 50, pp. 12186-12193
Publication Year
2014
Abstract
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 °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 (Δ3 and Δ11 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 γ-aminobutyrate in a broad range of pH values.
Keyword
C-terminal regionGABAGlutamate decarboxylaseLactobacillus plantarumPH dependence
ISSN
0021-8561
Publisher
Amer Chem Soc
DOI
http://dx.doi.org/10.1021/jf504656h
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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