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|Title:||Characterization of ß-xylosidase Enzyme from a Pichia Stipitis Mutant|
|Authors:||BASARAN Pervin; OZCAN Meltem|
|Citation:||BIORESOURCE TECHNOLOGY vol. 99 no. 1 p. 38-43|
|Publisher:||ELSEVIER SCI LTD|
|Type:||Articles in periodicals and books|
|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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