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Biosci Biotechnol Biochem. 2013;77(4):853-6. Epub 2013 Apr 7.

Expression and characterization of a glutamate decarboxylase from Lactobacillus brevis 877G producing γ-aminobutyric acid.

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1
Division of Bioengineering, University of Incheon, Incheon, Republic of Korea.

Abstract

The glutamate decarboxylase of γ-aminobutyric acid-producing Lactobacillus brevis 877G (LbGAD) was expressed in Escherichia coli. The optimal pH and temperature for the purified LbGAD activity were respectively determined to be pH 5.2 and 45 °C. CaCl2 was shown to be a potent activator of this LbGAD activity. The kinetic parameters for LbGAD were a Km value of 3.6 mmol/L and a Vmax value of 0.06 mmol/L/min for L-monosodium glutamate.

PMID:
23563537
DOI:
10.1271/bbb.120785
[Indexed for MEDLINE]
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