Expression and Characterization of a Glutamate Decarboxylase from Lactobacillus brevis 877G Producing γ-Aminobutyric Acid

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 K_m value of 3.6 mmol/L and a V_max value of 0.06 mmol/L/min for L-monosodium glutamate.