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 |