ArticleInternational journal of molecular sciences2013
Gamma-aminobutyric acid production using immobilized glutamate decarboxylase followed by downstream processing with cation exchange chromatography.
Article in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Production of γ-Aminobutyrate (GABA) in RecombinantACS omega · 2022Article
- Characterization of three glutamate decarboxylases from Bacillus spp. for efficient γ-aminobutyric acid production.Microbial cell factories · 2021Article
- Environmental Conditions Affecting GABA Production inMicroorganisms · 2021Article
- Hydrogel Film-Immobilized Lactobacillus brevis RK03 for γ-Aminobutyric Acid Production.International journal of molecular sciences · 2017Article
- Biotechnological advances and perspectives of gamma-aminobutyric acid production.World journal of microbiology & biotechnology · 2017Review
- On-line near-infrared spectroscopy optimizing and monitoring biotransformation process of γ-aminobutyric acid.Journal of pharmaceutical analysis · 2016Article
- Preparation of novel poly(hydroxyethyl methacrylate-co-glycidyl methacrylate)-grafted core-shell magnetic chitosan microspheres and immobilization of lactase.International journal of molecular sciences · 2013Article
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Authors and funding
6 authors.
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Abstract
We have developed a gamma-aminobutyric acid (GABA) production technique using his-tag mediated immobilization of Escherichia coli-derived glutamate decarboxylase (GAD), an enzyme that catalyzes the conversion of glutamate to GABA. The GAD was obtained at 1.43 g/L from GAD-overexpressed E. coli fermentation and consisted of 59.7% monomer, 29.2% dimer and 2.3% tetramer with a 97.6% soluble form of the total GAD. The harvested GAD was immobilized to metal affinity gel with an immobilization yield of 92%. Based on an investigation of specific enzyme activity and reaction characteristics, glutamic acid (GA) was chosen over monosodium glutamate (MSG) as a substrate for immobilized GAD, resulting in conversion of 2.17 M GABA in a 1 L reactor within 100 min. The immobilized enzymes retained 58.1% of their initial activities after ten consecutive uses. By using cation exchange chromatography followed by enzymatic conversion, GABA was separated from the residual substrate and leached GAD. As a consequence, the glutamic acid was mostly removed with no detectable GAD, while 91.2% of GABA was yielded in the purification step.
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