title: 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 Km value of 3.6 mmol/L and a Vmax value of 0.06 mmol/L/min for L-monosodium glutamate.
authors.affiliation: Division of Bioengineering, University of Incheon, Incheon, Republic of Korea.
authors.forename: Myung-Ji
authors.initials: MJ
authors.lastname: Seo
authors.forename: Young-Do
authors.initials: YD
authors.lastname: Nam
authors.forename: So-Young
authors.initials: SY
authors.lastname: Lee
authors.forename: So-Lim
authors.initials: SL
authors.lastname: Park
authors.forename: Sung-Hun
authors.initials: SH
authors.lastname: Yi
authors.forename: Seong-Il
authors.initials: SI
authors.lastname: Lim
mesh_terms: D004926:Escherichia coli / Q000235:genetics; D005285:Fermentation; D015870:Gene Expression; D005968:Glutamate Decarboxylase / Q000235:genetics* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D052196:Levilactobacillus brevis / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism*; D013696:Temperature; D005680:gamma-Aminobutyric Acid / Q000096:biosynthesis*
chemical_list: D005680:gamma-Aminobutyric Acid; D005968:Glutamate Decarboxylase