Production of γ-aminobutyric acid using immobilized glutamate decarboxylase from Lactobacillus plantarum

Sang Jae Lee; Han Seung Lee; Dong Woo Lee

doi:10.4014/mbl.1509.09003

Production of γ-aminobutyric acid using immobilized glutamate decarboxylase from Lactobacillus plantarum

Sang Jae Lee, Han Seung Lee, Dong Woo Lee

Department of Biotechnology

Research output: Contribution to journal › Article › peer-review

12 Citations (Scopus)

Abstract

The glutamate decarboxylase gene {gadB) from Lactobacillus plantarum WCFS1 was cloned and expressed as an N-terminal hexa-histidine-tagged fusion protein in Escherichia coli BL21 (DE3) as the host strain. Purified glutamate decarboxylase (GAD) was immobilized onto porous silica beads by covalent coupling. The pH dependence of activity and stability of the immobilized GAD was significantly altered, when compared to those of the free enzyme. Immobilized GAD was stable in the range of pH 3.5 to 6.0. The resulting packed-bed reactor produced 41.7 g of γ-aminobutyric acid/Ih at 45°C.

Original language	English
Pages (from-to)	300-305
Number of pages	6
Journal	Korean Journal of Microbiology and Biotechnology
Volume	43
Issue number	3
DOIs	https://doi.org/10.4014/mbl.1509.09003
Publication status	Published - 2015 Sept

Bibliographical note

Publisher Copyright:
© 2015, The Korean Society for Microbiology and Biotechnology.

All Science Journal Classification (ASJC) codes

Biotechnology
Microbiology
Applied Microbiology and Biotechnology

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10.4014/mbl.1509.09003

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title = "Production of γ-aminobutyric acid using immobilized glutamate decarboxylase from Lactobacillus plantarum",

abstract = "The glutamate decarboxylase gene {gadB) from Lactobacillus plantarum WCFS1 was cloned and expressed as an N-terminal hexa-histidine-tagged fusion protein in Escherichia coli BL21 (DE3) as the host strain. Purified glutamate decarboxylase (GAD) was immobilized onto porous silica beads by covalent coupling. The pH dependence of activity and stability of the immobilized GAD was significantly altered, when compared to those of the free enzyme. Immobilized GAD was stable in the range of pH 3.5 to 6.0. The resulting packed-bed reactor produced 41.7 g of γ-aminobutyric acid/Ih at 45°C.",

keywords = "Glutamate decarboxylase, Immobilization, Lactobacillus plantarum, Packed-bed reactor, Y-aminobutyric acid",

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AU - Lee, Sang Jae

AU - Lee, Han Seung

AU - Lee, Dong Woo

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N2 - The glutamate decarboxylase gene {gadB) from Lactobacillus plantarum WCFS1 was cloned and expressed as an N-terminal hexa-histidine-tagged fusion protein in Escherichia coli BL21 (DE3) as the host strain. Purified glutamate decarboxylase (GAD) was immobilized onto porous silica beads by covalent coupling. The pH dependence of activity and stability of the immobilized GAD was significantly altered, when compared to those of the free enzyme. Immobilized GAD was stable in the range of pH 3.5 to 6.0. The resulting packed-bed reactor produced 41.7 g of γ-aminobutyric acid/Ih at 45°C.

AB - The glutamate decarboxylase gene {gadB) from Lactobacillus plantarum WCFS1 was cloned and expressed as an N-terminal hexa-histidine-tagged fusion protein in Escherichia coli BL21 (DE3) as the host strain. Purified glutamate decarboxylase (GAD) was immobilized onto porous silica beads by covalent coupling. The pH dependence of activity and stability of the immobilized GAD was significantly altered, when compared to those of the free enzyme. Immobilized GAD was stable in the range of pH 3.5 to 6.0. The resulting packed-bed reactor produced 41.7 g of γ-aminobutyric acid/Ih at 45°C.

KW - Glutamate decarboxylase

KW - Immobilization

KW - Lactobacillus plantarum

KW - Packed-bed reactor

KW - Y-aminobutyric acid

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Production of γ-aminobutyric acid using immobilized glutamate decarboxylase from Lactobacillus plantarum

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

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