ArticleAmino acids2020
Immobilization and enzymatic properties of glutamate decarboxylase from Enterococcus faecium by affinity adsorption on regenerated chitin.
Article in Amino acids, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 9 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
- Construction of a co-reaction system for ethanol-promoted gamma-aminobutyric acid synthesis by Pediococcus pentosaceus.Amino acids · 2025Article
- Molecular Analysis of Glutamate Decarboxylases inFrontiers in microbiology · 2021Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Glutamate decarboxylase (GAD, EC 4.1.1.15) is an important enzyme in gamma-aminobutyric acid biosynthesis and DL-glutamic acid resolution. In this study, the Enterococcus faecium-derived GAD was successfully immobilized by regenerated chitin (RC) via specific adsorption of cellulose-binding domain (CBD). The optimal binding buffer was 20 mmol/L phosphate buffer saline (pH 8.0), and the RC binding capacity was 1.77 ± 0.11 mg
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