Characterization of three glutamate decarboxylases from Bacillus spp. for efficient γ-aminobutyric acid production.

ABSTRACT:

Background

Gamma-aminobutyric acid (GABA) is an important bio-product used in pharmaceuticals and functional foods and as a precursor of the biodegradable plastic polyamide 4. Glutamate decarboxylase (GAD) converts L-glutamate (L-Glu) into GABA via decarboxylation. Compared with other methods, develop a bioconversion platform to produce GABA is of considerable interest for industrial use.

Results

Three GAD genes were identified from three Bacillus strains and heterologously expressed in Escherichia coli BL21 (DE3). The optimal reaction temperature and pH values for three enzymes were 40 °C and 5.0, respectively. Of the GADs, GADZ11 had the highest catalytic efficiency towards L-Glu (2.19 mM^- 1 s^- 1). The engineered E. coli strain that expressed GADZ11 w

SUBMITTER: Sun L 

PROVIDER: S-EPMC8336373 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature