ArticleApplied microbiology and biotechnology2021
Reconstruction of the glutamate decarboxylase system in Lactococcus lactis for biosynthesis of food-grade γ-aminobutyric acid.
Article in Applied microbiology and biotechnology, 2021. 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, 26 citations in OpenAlex.
- Probiotic attributes, antioxidant and neuromodulatory effects of GABA-Producing Lactiplantibacillus plantarum SY1 and optimization of GABA production.BMC microbiology · 2025Article
- The Anti-Inflammatory Effect ofInternational journal of molecular sciences · 2024Article
- Contributions of Gamma-Aminobutyric Acid (GABA) Produced by Lactic Acid Bacteria on Food Quality and Human Health: Current Applications and Future Prospects.Foods (Basel, Switzerland) · 2024Review
- Expression and Transformation Characteristics of a Novel Glutamic Acid Decarboxylase LcGAD10s and Its Application on Sufu Processing.Foods (Basel, Switzerland) · 2023Article
- High-level production of γ-aminobutyric acid via efficient co-expression of the key genes of glutamate decarboxylase system inEngineering microbiology · 2023Article
- Sodium-Ion-Free Fermentative Production of GABA withMetabolites · 2023Article
- Molecular evolution and population genetics of glutamate decarboxylase acid resistance pathway in lactic acid bacteria.Frontiers in genetics · 2023Article
- Expression, purification, and characterization of glutamate decarboxylase from human gut-originated Lactococcus garvieae MJF010.World journal of microbiology & biotechnology · 2022Article
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
Abstract
Gamma-aminobutyric acid (GABA), an important bioactive compound, is synthesized through the decarboxylation of L-glutamate (L-Glu) by glutamate decarboxylase (GAD). The use of lactic acid bacteria (LAB) as catalysts opens interesting avenues for the biosynthesis of food-grade GABA. However, a key obstacle involved in the improvement of GABA production is how to resolve the discrepancy of optimal pH between the intracellular GAD activity and cell growth. In this work, a potential GAD candidate (LpGadB) from Lactobacillus plantarum was heterologously expressed in Escherichia coli. Recombinant LpGadB existed as a homodimer under the native conditions with a molecular mass of 109.6 kDa and exhibited maximal activity at 40°C and pH 5.0. The K
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Registered trials
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