ArticleWorld journal of microbiology & biotechnology2022
Expression, purification, and characterization of glutamate decarboxylase from human gut-originated Lactococcus garvieae MJF010.
Article in World journal of microbiology & biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Coordinated Regulation of Glutamate-GABA Flux Enables High-Titre GABA Production in Enterococcus faecium.Applied biochemistry and biotechnology · 2026Article
- GABA-Producing Bacteria as Potential Psychobiotics in Gut-Brain Axis Regulation.International journal of molecular sciences · 2026Review
- Isolation of a Gamma-Aminobutyric Acid (GABA)-ProducingFood science & nutrition · 2026Article
- Unraveling the Potential of γ-Aminobutyric Acid: Insights into Its Biosynthesis and Biotechnological Applications.Nutrients · 2024Review
- Gamma-aminobutyric acid as a potential postbiotic mediator in the gut-brain axis.NPJ science of food · 2024Review
- Expression and Transformation Characteristics of a Novel Glutamic Acid Decarboxylase LcGAD10s and Its Application on Sufu Processing.Foods (Basel, Switzerland) · 2023Article
- Sodium-Ion-Free Fermentative Production of GABA withMetabolites · 2023Article
- Expanding the pH range of glutamate decarboxylase fromFrontiers in bioengineering and biotechnology · 2023Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Human gut-originated lactic acid bacteria were cultivated, and high γ-aminobutyric acid (GABA)-producing Lactococcus garvieae MJF010 was identified. To date, despite the importance of GABA, no studies have investigated GABA-producing Lactococcus species, except for Lc. lactis. A recombinant glutamate decarboxylase of the strain MJF010 (rLgGad) was successfully expressed in Escherichia coli BL21(DE3) with a size of 53.9 kDa. rLgGad could produce GABA, which was verified using the silylation-derivative fragment ions of GABA. The purified rLgGad showed the highest GABA-producing activity at 35 °C and pH 5. rLgGad showed a melting temperature of 43.84 °C. At 30 °C, more than 80% of the activity was maintained even after 7 h; however, it rapidly decreased at 50 °C. The kinetic parameters, K
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