Lp_3485, an α-D-galactosidase from Lactobacillus plantarum WCFs1: production and biochemical characterization

Póster presentado a la VII International Conference on Environmental Industrial and Applied Microbiology, celebrada en Madrid (España) del 18 al 20 de octubre de 2017.Glycosil hydrolases are classified into the sequence-based CAZY database (http://www.cazy.org) in families organized in mechanistically and structurally related clans. α-Galactosidases belong to families GH4, 27, 36, 57, 97 and 110. GH27 and 36 have been subjected to extensive biochemical characterization owing to their importance for industrial applications. Some foods, like legumes, contain α-galactosides possessing one or several galactose units, linked together or to the glucose moiety of sucrose though α-1, 6 linkages. Several microorganisms are known to produce α-galactosidases. Lactic acid bacteria, used in vegetable fermentations, can hydrolyze α-galactosides to digestible carbohydrates. The aim of this study was to characterize an α-galactosidase from the lactic acid bacterium Lactobacillus plantarum WCFS1, therefore the lp_3485 gene encoding a putative α-galactosidase was cloned and the recombinant protein was hiperproduced, purified, and biochemically characterized. Substrate specificity was assayed against a library of 4-nitrophenyl synthetic glycosides. As expected, the results confirmed that Lp_3485 was able to hydrolyze 4-nitrophenyl-α-Dgalactopyranoside. The use of Mn2+ and Fe2+ ions, triton-X-100, tween 20, DECP and EDTA greatly increased Lp_3485 activity. This α-galactosidase from L. plantarum could be used to enhance the digestibility of food α-galactosides.This work was supported by grant AGL2014-52911-R (MINEICO).Peer Reviewe