Substrate Binding by the Catalytic Domain and Carbohydrate Binding Module of Ruminococcus flavefaciens FD-1 Xyloglucanase/ Endoglucanase

dc.contributor.author Warner, Christopher
dc.contributor.author Camci-Unal, Gulden
dc.contributor.author Reilly, Peter
dc.contributor.author Pohl, Nicola
dc.contributor.author Ford, Clark
dc.contributor.author Reilly, Peter
dc.contributor.department Chemical and Biological Engineering
dc.date 2018-02-13T03:06:46.000
dc.date.accessioned 2020-06-30T01:10:40Z
dc.date.available 2020-06-30T01:10:40Z
dc.date.copyright Sun Jan 01 00:00:00 UTC 2012
dc.date.embargo 2012-11-09
dc.date.issued 2013-01-09
dc.description.abstract <p>Binding and thermodynamic properties of a carbohydrate binding module (CBM) and a glycoside hydrolase family 44 xyloglucanase/endoglucanase catalytic domain (CD) from<em>Ruminococcus flavefaciens</em>, both when separate and when linked to each other, have been quantified when binding various β-1,4-linked glucans and xylans. The three constructs bind cellotetraose, cellopentaose, and cellohexaose with association constants that increase with chain length. The CBM does not bind xylotetraose, xylopentaose, or xylohexaose. The CD appears to bind carboxymethylcellulose (CMC) and xylan only weakly, while the CBM and the CD/CBM bind them much more strongly than they bind the cellooligosaccharides. CMC is bound to a much greater degree than is xylan. Association constants for the cellooligosaccharides are in the order CBM CD < CD/CBM, while those on CMC and xylan are CD CBM CD/CBM. A synergistic effect was observed for the association constants of cellopentaose and cellohexaose with the CD/CBM when compared to the CD and CBM alone. Binding of all ligands by all three constructs is energetically favorable, enthalpy-driven, and subject to enthalpy–entropy compensation.</p>
dc.description.comments <p>Posted with permission from <em>Industrial & Engineering Chemistry Research</em>, 52, no. 1 (2013): 30–36, doi:<a href="http://dx.doi.org/10.1021/ie202988a" target="_blank">10.1021/ie202988a</a>. Copyright 2012 American Chemical Society.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/cbe_pubs/6/
dc.identifier.articleid 1007
dc.identifier.contextkey 3459575
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath cbe_pubs/6
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/13559
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/cbe_pubs/6/ie202988a.pdf|||Sat Jan 15 01:04:54 UTC 2022
dc.source.uri 10.1021/ie202988a
dc.subject.disciplines Biochemical and Biomolecular Engineering
dc.subject.disciplines Biological Engineering
dc.subject.disciplines Chemical Engineering
dc.subject.disciplines Food Chemistry
dc.subject.disciplines Food Science
dc.subject.disciplines Plant Sciences
dc.title Substrate Binding by the Catalytic Domain and Carbohydrate Binding Module of Ruminococcus flavefaciens FD-1 Xyloglucanase/ Endoglucanase
dc.type article
dc.type.genre article
dspace.entity.type Publication
relation.isAuthorOfPublication 0727532a-2892-42e2-84ab-5af5088f76c6
relation.isOrgUnitOfPublication 86545861-382c-4c15-8c52-eb8e9afe6b75
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