ArticleInternational journal of molecular sciences2012
Expression, immobilization and enzymatic properties of glutamate decarboxylase fused to a cellulose-binding domain.
Article in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Physical entrapment of glutamic acid decarboxylase from Lactobacillus casei IIB-09 in multifunctional mesoporous silica nanoparticles for controlled release of ɣ-aminobutyric acid in anxiety disorders.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- High Production of γ-Aminobutyric Acid by Activating theACS omega · 2023Article
- Glutamate Decarboxylase from Lactic Acid Bacteria-A Key Enzyme in GABA Synthesis.Microorganisms · 2020Review
- Immobilization and enzymatic properties of glutamate decarboxylase from Enterococcus faecium by affinity adsorption on regenerated chitin.Amino acids · 2020Article
- Enzymatic kinetic resolution of desmethylphosphinothricin indicates that phosphinic group is a bioisostere of carboxyl group.Communications chemistry · 2020Article
- 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
- Gamma-aminobutyric acid production using immobilized glutamate decarboxylase followed by downstream processing with cation exchange chromatography.International journal of molecular sciences · 2013Article
- Preparation of a Cu(II)-PVA/PA6 composite nanofibrous membrane for enzyme immobilization.International journal of molecular sciences · 2012Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli-derived glutamate decarboxylase (GAD), an enzyme that catalyzes the conversion of glutamic acid to gamma-aminobutyric acid (GABA), was fused to the cellulose-binding domain (CBD) and a linker of Trichoderma harzianum endoglucanase II. To prevent proteolysis of the fusion protein, the native linker was replaced with a S(3)N(10) peptide known to be completely resistant to E. coli endopeptidase. The CBD-GAD expressed in E. coli was successfully immobilized on Avicel, a crystalline cellulose, with binding capacity of 33 ± 2 nmol(CBD-GAD)/g(Avicel) and the immobilized enzymes retained 60% of their initial activities after 10 uses. The results of this report provide a feasible alternative to produce GABA using immobilized GAD through fusion to CBD.
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