Title: Characterization of ß-xylosidase Enzyme from a Pichia Stipitis Mutant
Authors: BASARAN PervinOZCAN Meltem
Citation: BIORESOURCE TECHNOLOGY vol. 99 no. 1 p. 38-43
Publisher: ELSEVIER SCI LTD
Publication Year: 2008
JRC Publication N°: JRC35915
ISSN: 0960-8524
URI: http://www.sciencedirect.com
http://publications.jrc.ec.europa.eu/repository/handle/JRC35915
DOI: 10.1016/j.biortech.2006.11.056
Type: Articles in Journals
Abstract: b-Xylosidase production was maximal for the mutant Pichia stipitis NP54376 grown on xylan as the sole carbon source. b-Xylosidase was purified from culture supernatant by (NH4)2SO4 precipitation and a hydrophobic interaction chromatography on phenyl sepharose. Optima of pH and temperature were 5.0 and 50 C, respectively. The enzyme was inhibited by 2-mercaptoethanol (100%) and Fe3+ (80%), and moderately affected by Cu2+, Ag+, NHþ4 and Mg2+ and SDS. The purified xylosidase hydrolyzed xylobiose and xylo-oligosaccharides and it did not exhibit activity against cellulose, starch, maltose and cellobiose. 2.5 g l1 glucose repressed b-xylosidase activity in the NP54376 strain. The Km and Vmax values on p-nitrophenyl-b-xylopyranoside were 1.6 mM and 186 lmol p-nitrophenyl min1 mg1 protein, respectively. Analysis of the hydrolysis products by HPLC indicated that the major hydrolysis product is xylobiose in all the carbon sources tested.
JRC Institute:Institute for Prospective Technological Studies

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