Screening for glycosidase activities of lactic acid bacteria as a biotechnological tool in oenology

Abstract

The aim of this study was to evaluate the ability from a number of lactic acid bacteria isolated from different sources to produce glycosidase enzymes. Representative isolates (225) from clusters obtained after genotyping, using randomly amplified polymorphic DNA-polymerase chain reaction (RAPD-PCR) analysis, of 1,464 isolates, were screened for β-D-glucosidase activity. Thirty-five of them were selected for subsequent analysis. These strains were able to hydrolyze α-D-glucopyranoside, β-D-xylopyranoside and α-L-arabinofuranoside although β-D-glucosidase activity was the predominant activity for 22 of the selected strains. Only some of them did so with α-L-rhamnopyranoside. All of these were from wine samples and were identified as belonging to the Oenococcus oeni species using Amplification and Restriction Analysis of 16S-rRNA gene (16S-ARDRA). When the influence of pH, temperature and ethanol or sugars content on β-D-glucosidase activity was assayed, a strain-dependent response was observed. The β-D-glucosidase activity occurred in both whole and sonicated cells but not in the supernatants from cultures or obtained after cell sonication. Strains 10, 17, 21, and 23 retained the most β-D-glucosidase activity when they were assayed at the conditions of temperature, pH, ethanol and sugar content used in winemaking. These results suggest that these strains could be used as a source of glycosidase enzymes for use in winemaking.

Identification and Localization of β-D-Glucosidase from Two Typical Oenococcus oeni Strains

“…As for location of βG, intracellular enzyme has been reported for different O. oeni strains (Barbagallo et al, 2004;Michlmayr et al, 2010;Perez-Martin et al, 2012). The same results have also been observed for O. oeni SD-2a and 31MBR (Li et al, 2012b).…”

“…However, the subcellular localization prediction showed the enzyme exists mainly in the cytoplasm as a soluble protein, which may be due to the secondary and tertiary structure of the protein that alters the hydrophobicity of βG. βG of the two strains was predicted as a non-secretory protein which mirrors the previous report that low βG activity was observed in the culture supernatant for both strains (Li et al, 2012b), as well as the subcellular localization prediction that little of the enzyme was extracellular.As for location of βG, intracellular enzyme has been reported for different O. oeni strains (Barbagallo et al, 2004;Michlmayr et al, 2010;Perez-Martin et al, 2012). The same results have also been observed for O. oeni SD-2a and 31MBR (Li et al, 2012b).…”

Enzymes for Wine Fermentation: Current and Perspective Applications

“…Perez-Martin et al [41] studied >1000 isolates for glycosidases. The β-glucosidase activities were only found in cells, but not in the supernatants of the cultures.…”

Use ofKluyveromyces marxianusprefermented wheat bran as a source of enzyme mixture to improve dough performance and bread biochemical properties

“…During fermentation, K. marxianus yeast isolated from several habitats releases cellulose-degrading enzymes such as xylanase, endoglucanase, exoglucanase, and β-glucosidase (Yan et al, 2015). In microorganisms like lactic acid bacteria (LAB), few strains show high intracellular β-glucosidase activity (Michlmayr, Schumann, Braz da Silva, Kulbe, & Hierro, 2010), with almost no extracellular β-glucosidase activity reported (Perez-Martin, Sesena, Izquierdo, Martin, & Palop, 2012). In microorganisms like lactic acid bacteria (LAB), few strains show high intracellular β-glucosidase activity (Michlmayr, Schumann, Braz da Silva, Kulbe, & Hierro, 2010), with almost no extracellular β-glucosidase activity reported (Perez-Martin, Sesena, Izquierdo, Martin, & Palop, 2012).…”