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Characterization of beta-xylosidase enzyme from a Pichia stipitis mutant

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dc.creator Basaran, Pervin
dc.creator Ozcan, Meltem
dc.date 2008-01-01T01:00:00Z
dc.date.accessioned 2021-12-03T11:15:31Z
dc.date.available 2021-12-03T11:15:31Z
dc.identifier 15caf4f9-fdbf-47c4-8b1e-42b6d7a04577
dc.identifier 10.1016/j.biortech.2006.11.056
dc.identifier https://avesis.sdu.edu.tr/publication/details/15caf4f9-fdbf-47c4-8b1e-42b6d7a04577/oai
dc.identifier.uri http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/90103
dc.description p-Xylosidase production was maximal for the mutant Pichia stipitis NP54376 grown on xylan as the sole carbon source. P-Xylosidase was purified from culture supernatant by (NH4)(2)SO4 precipitation and a hydrophobic interaction chromatography on phenyl sepharose. Optima of pH and temperature were 5.0 and 50 degrees C, respectively. The enzyme was inhibited by 2-mercaptoethanol (100%) and Fe3+ (80%), and moderately affected by Cu2+, Ag+, NH4+ 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 l(-1) glucose repressed P-xylosidase activity in the NP54376 strain. The K-m and V-max values on p-nitrophenyl-p-xylopyranoside were 1.6 mM and 186 mu mol p-nitrophenyl min(-1) mg(-1) protein, respectively. Analysis of the hydrolysis products by HPLC indicated that the major hydrolysis product is xylobiose in all the carbon sources tested. (C) 2006 Elsevier Ltd. All rights reserved.
dc.language eng
dc.rights info:eu-repo/semantics/closedAccess
dc.title Characterization of beta-xylosidase enzyme from a Pichia stipitis mutant
dc.type info:eu-repo/semantics/article


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