Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

A Brief Review on Glutamate Decarboxylase From Lactic Acid Bacteria

Version 1 : Received: 26 October 2020 / Approved: 27 October 2020 / Online: 27 October 2020 (08:38:21 CET)

How to cite: Yogeswara, I.B.A.; Maneerat, S.; Haltrich, D. A Brief Review on Glutamate Decarboxylase From Lactic Acid Bacteria. Preprints 2020, 2020100538 (doi: 10.20944/preprints202010.0538.v1). Yogeswara, I.B.A.; Maneerat, S.; Haltrich, D. A Brief Review on Glutamate Decarboxylase From Lactic Acid Bacteria. Preprints 2020, 2020100538 (doi: 10.20944/preprints202010.0538.v1).

Abstract

Glutamate decarboxylase (L-glutamate-1-carboxylase, GAD; EC 4.1.1.15) is a pyridoxal 5-phosphate-dependent enzyme, which catalyzes the irreversible α-decarboxylation of L-glutamic acid to γ-aminobutyric acid (GABA) and CO2. The enzyme is widely distributed in eukaryotes as well as prokaryotes, where it – together with its reaction product GABA - fulfils very different physiological functions. The occurrence of gad genes encoding GAD has been shown for many microorganisms, and GABA-producing lactic acid bacteria (LAB) have been a focus of research during recent years. A wide range of traditional foods produced by fermentation based on LAB offer the potential of providing new functional food products enriched with GABA that may offer certain health-benefits. Different GAD enzymes and genes from several strains of LAB have been isolated and characterized recently. GABA-producing LAB, biochemical properties of their GAD enzymes, and possible applications are reviewed here.

Subject Areas

γ-aminobutyric acid; lactic acid bacteria; glutamate decarboxylase; fermented foods; GAD genes

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