The activity of family 11 xylanases at alkaline pH

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dc.contributor.author Gibbs, MD en
dc.contributor.author Reeves, RA en
dc.contributor.author Sowden, Elizabeth en
dc.contributor.author Choudhary, RR en
dc.contributor.author Daniel, RM en
dc.contributor.author Bergquist, Peter en
dc.date.accessioned 2011-07-24T21:45:30Z en
dc.date.issued 2010-12-31 en
dc.identifier.citation NEW BIOTECHNOL 27(6):795-802 31 Dec 2010 en
dc.identifier.issn 1871-6784 en
dc.identifier.uri http://hdl.handle.net/2292/7058 en
dc.description.abstract Xylanases have several industrial uses, particularly in baking, modification of animal feed and in pulp bleaching in the paper industry Process conditions in kraft pulp bleaching generally favour an enzyme that is active at high pH values The activities of several glycosyl hydrolase family 11 xylanases reported to be active under alkaline conditions were determined under optimal conditions and found to have optima in the pH 5-6 range Only one enzyme tested, BadX, was shown to have an alkaline pH optimum Significant activity at pH values higher than 8 appears often to be the result of excess enzyme added to the reaction mixtures so that substrate is limiting The different nature of laboratory and industrial substrates needs to be taken into consideration in designing assay conditions In some cases, significant differences were observed in pH profiles generated using a small-molecule substrate when compared to those generated using xylan We conclude that small-molecule substrates are not a suitable proxy for determining the pH profiles of family 11 xylanases en
dc.language EN en
dc.publisher ELSEVIER SCIENCE BV en
dc.relation.ispartofseries NEW BIOTECHNOL en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/1871-6784/ en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.subject AMINO-ACID SUBSTITUTION en
dc.subject GLYCOSIDE HYDROLASE en
dc.subject CATALYTIC-ACTIVITY en
dc.subject BACILLUS en
dc.subject MUTAGENESIS en
dc.subject PULP en
dc.subject EVOLUTION en
dc.subject INDUSTRY en
dc.subject BINDING en
dc.subject DOGS en
dc.title The activity of family 11 xylanases at alkaline pH en
dc.type Journal Article en
dc.identifier.doi 10.1016/j.nbt.2010.06.004 en
pubs.issue 6 en
pubs.begin-page 795 en
pubs.volume 27 en
dc.rights.holder Copyright: 2010 Elsevier B.V. en
dc.identifier.pmid 20601264 en
pubs.end-page 802 en
dc.rights.accessrights http://purl.org/eprint/accessRights/RestrictedAccess en
pubs.subtype Article en
pubs.elements-id 206856 en
pubs.org-id Libraries & Learning Services en
pubs.org-id Libraries & Learning Services en
pubs.org-id Research and Collections en
pubs.org-id Research and Collections en
pubs.org-id Research Services en
pubs.org-id Research Services en
pubs.record-created-at-source-date 2011-07-25 en
pubs.dimensions-id 20601264 en


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