Characterization of β-glucosidase activity of a Lactiplantibacillus plantarum 6-phospho-β-glucosidase

Abstract

β-Glucosidases are useful for hydrolysis of glycosidically-bound volatiles (GBV), thereby facilitating the release of aroma chemicals from the fruit matrices. In this study, 10 putative glycosyl hydrolases belonging to GH1 family from Lactiplantibacillus plantarum NCIM 2903 were cloned and recombinantly expressed. Interestingly, only one (LpBgl5) of the nine soluble proteins, previously characterized as a 6-phospho-β-glucosidase showed β-glucosidase activity which was further characterized. The enzyme had an optimum pH and temperature of 6 and 40°C, respectively, and was categorized as aryl-β-glucosidase due to its ability to hydrolyze different natural as well as synthetic glucosides except cellobiose. The enzyme exhibited functional activity across multiple substrates, with relative activity decreasing sequentially from β-xylosidase to β-glucosidase and finally β-mannosidase. The β-xylosidase and β-glucosidase activities of LpBgl5 were stimulated up to 300% and 700% in the presence of 4 M xylose and 4 M glucose, respectively. The enzyme could also hydrolyze GBV from mango. To our knowledge, this is the first recombinant β-glucosidase/β-xylosidase/β-mannosidase from L. plantarum to have potential for aroma enhancement in fruit products.

• A recombinant β-glycosidase from Lactiplantibacillus plantarum was characterized.

• The enzyme showed higher β-xylosidase activity than β-glucosidase activity.

• The enzyme could also hydrolyze glycosidically bound volatiles from mango.