Beta-glucosidase from the grape native yeast Debaryomyces vanrijiae: purification, characterization, and its effect on monoterpene content of a Muscat grape juice

J Agric Food Chem. 2003 Feb 26;51(5):1453-9. doi: 10.1021/jf025777l.

Abstract

Six hundred ten yeast colonies isolated from various vineyards in Chile were screened for the presence of a beta-glucosidase activity as well as the resistance to glucose and ethanol inhibition. Among them, Debaryomyces vanrijiae was found to produce high levels of an extracelular beta-glucosidase which was tolerant to glucose (K(i) = 439 mM) and ethanol inhibitions. The enzyme (designated DV-BG) was purified to apparent homogeneity, respectively, by gel filtration, ion-exchange, and chromatofocusing techniques. Its molecular weight was 100 000, and its pI 3.0, optimum pH, and temperature activities were 5.0 and 40 degrees C, respectively, and had a V(max) of 47.6 micromol min(-)(1) mg(-)(1) and a K(m) of 1.07 mM. The enzyme was active against different beta-d-glucosides including glucosidic flavor precursors. The disaccharidic flavor precursors were not substrates for the enzyme. When added to a Muscat grape juice, the concentration of several monoterpenes increased as the consequence of its hydrolytic activity.

MeSH terms

  • Ascomycota / enzymology*
  • Beverages / analysis*
  • Chromatography
  • Fruit / chemistry*
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Kinetics
  • Molecular Weight
  • Monoterpenes / analysis*
  • Monoterpenes / metabolism
  • Substrate Specificity
  • Temperature
  • Vitis / chemistry*
  • beta-Glucosidase / chemistry
  • beta-Glucosidase / isolation & purification*
  • beta-Glucosidase / metabolism*

Substances

  • Monoterpenes
  • beta-Glucosidase