title: Purification and characterization of the endocellular beta-glucosidase of a new strain of Candida entomophila isolated from fermenting agave (Agave sp.) juice.
abstract: A yeast strain isolated in the laboratory from fermenting agave (Agave sp.) juice was studied and classified as Candida entomophila. The beta-glucosidase of this yeast was purified by ion-exchange chromatography and gel filtration. Its molecular mass estimated by gel filtration was 400 kDa. The oligomeric structure was determined following treatment of the purified enzyme with SDS. Its optimum pH was between 5 and 6, and its optimum temperature was 60 degrees C. The enzyme was active against soluble glucosides with (1-->3)-beta, (1-->4)-beta and (1-->4)-alpha linkage configuration, and it possesses (1-->6)-alpha-arabinofuranosidase activity. It is competitively inhibited by glucose and by D-gluconic acid lactone. The enzyme was constitutive and a glucosyltransferase activity is observed in the presence of ethanol. Since the glycosides present in wines and fruit juices represent a potential source of aromatic flavour, the possible use of the yeast glucosidase for the liberation of the bound aroma is discussed.
authors.affiliation: Ecole Nationale Supérieure Agronomique de Montpellier, France.
authors.forename: Y
authors.initials: Y
authors.lastname: Gueguen
authors.forename: P
authors.initials: P
authors.lastname: Chemardin
authors.forename: A
authors.initials: A
authors.lastname: Arnaud
authors.forename: P
authors.initials: P
authors.lastname: Galzy
mesh_terms: D002175:Candida / Q000201:enzymology*; D005285:Fermentation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009812:Odorants; D010946:Plants, Medicinal / Q000378:metabolism* / Q000382:microbiology; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity; D013696:Temperature; D001617:beta-Glucosidase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification*
chemical_list: D001617:beta-Glucosidase