Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 62, Issue 50, Pages 12186-12193Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf504656h
Keywords
pH dependence; glutamate decarboxylase; C-terminal region; GABA; Lactobacillus plantarum
Funding
- National Agenda Program for Agricultural R&D from the Rural Development Administration [PJ0097672014]
- National Research Foundation of Korea, South Korea [NRF-2012R1A1A2042114]
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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.
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