원문정보
초록
영어
Gamma aminobutyric acid (GABA) is not only an essential inhibitory neurotransmitter which has a lot of physiological functions in humans but also a major monomer for a biobased and biodegradable polymer, polyamide 4. From an industrial point of view, the production of
GABA from the cheap source such as L-glutamate (L-MSG) is a completely reasonable and valuable process. The process can be well catalyzed by the enzyme glutamate decarboxylase (GAD) gained from various microorganism resources. In this work, we have conducted the α-decarboxylation of glutamate to yield GABA using pyridoxal phosphate-dependent GAD extracted from Escherichia coli. In order to obtain the intracellular enzyme, the strain was cultivated for 24
hours at 37 oC in LB medium and then sonicated, and the GAD was partially purified from the cell extract. The GAD showed a catalytic activity toward the conversion of L-MSG into GABA. With this
glutamate decarboxylase from E. coli, effects of reaction conditions such as temperature, pH, and substrate concentration were examined.