Preprint
Review

A Brief Review on Glutamate Decarboxylase From Lactic Acid Bacteria

Altmetrics

Downloads

374

Views

376

Comments

0

A peer-reviewed article of this preprint also exists.

Submitted:

26 October 2020

Posted:

27 October 2020

You are already at the latest version

Alerts
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.
Keywords: 
Subject: Biology and Life Sciences  -   Biochemistry and Molecular Biology
Copyright: This open access article is published under a Creative Commons CC BY 4.0 license, which permit the free download, distribution, and reuse, provided that the author and preprint are cited in any reuse.
Prerpints.org logo

Preprints.org is a free preprint server supported by MDPI in Basel, Switzerland.

Subscribe

© 2024 MDPI (Basel, Switzerland) unless otherwise stated