Glutathione biosynthesis and activity of dependent enzymes in food-grade lactic acid bacteria harbouring multidomain bifunctional fusion gene (gshF).

Abstract

To assess glutathione (GSH) biosynthesis ability and activity of dependent enzymes in food-grade lactic acid bacteria (LAB) and correlating with genomic information on GSH system in LAB. Whole-genome sequences of 26 food-grade LAB were screened for the presence/absence of a set of genes involved in de novo GSH system. Multiple strains of Streptococcus thermophilus (37), Lactobacillus casei (37), Lactobacillus rhamnosus (4), Lactobacillus paracasei (8) Lactobacillus plantarum (23) and Lactobacillus fermentum (22) were screened for biochemical evidence of the GSH system. Multiple sequence analysis of GshF sequences was carried out for comparing the genomic signatures between GSH-producing and nonproducing species. Streptococcus thermophilus was found to have de novo GSH biosynthesis as well as import ability. Lactobacillus sp. were negative for GSH synthesis but could import it from the medium. All the species exhibited prolific GSH reductase and peroxidase activity. Sequence analysis revealed the absence of key amino acid residues as well as a truncated N-terminal region in lactobacilli. The study provides a comprehensive view on the status of an important antioxidative system (the GSH system) in LAB and is expected to serve as a primer for future work on the mechanistic role of GSH in the group.