title: Heterologously expressed family 51 alpha-L-arabinofuranosidases from Oenococcus oeni and Lactobacillus brevis.
abstract: Putative α-L-arabinofuranosidases of Oenococcus oeni and Lactobacillus brevis were heterologously expressed and characterized. We report the basic functional properties of the recombinant enzymes in comparison to those of a commercial family 51 arabinosidase of Aspergillus niger.
authors.affiliation: Department of Food Sciences and Technology, Division of Food Biotechnology, University of Natural Resources and Life Sciences, Vienna, Muthgasse 11, A-1190 Vienna, Austria. herbert.michlmayr@boku.ac.at
authors.forename: Herbert
authors.initials: H
authors.lastname: Michlmayr
authors.forename: Christina
authors.initials: C
authors.lastname: Schümann
authors.forename: Klaus D
authors.initials: KD
authors.lastname: Kulbe
authors.forename: Andrés M
authors.initials: AM
authors.lastname: del Hierro
mesh_terms: D001234:Aspergillus niger / Q000201:enzymology / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D052196:Levilactobacillus brevis / Q000201:enzymology* / Q000235:genetics*; D008969:Molecular Sequence Data; D056585:Oenococcus / Q000201:enzymology* / Q000235:genetics*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; C019713:alpha-N-arabinofuranosidase