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dc.contributor.authorHamre, Anne Grethe
dc.contributor.authorStrømnes, Anne-Grethe
dc.contributor.authorGustavsen, Daniel
dc.contributor.authorVaaje-Kolstad, Gustav
dc.contributor.authorEijsink, Vincent
dc.contributor.authorSørlie, Morten
dc.date.accessioned2020-11-26T14:15:25Z
dc.date.available2020-11-26T14:15:25Z
dc.date.created2019-01-17T12:27:07Z
dc.date.issued2019
dc.identifier.issn0008-6215
dc.identifier.urihttps://hdl.handle.net/11250/2689829
dc.description.abstractProcessive glycoside hydrolases associate with recalcitrant polysaccharides such as cellulose and chitin and repeatedly cleave glycosidic linkages without fully dissociating from the crystalline surface. The processive mechanism is efficient in the degradation of insoluble substrates, but comes at the cost of reduced enzyme speed. We show that less processive chitinase variants with reduced ability to degrade crystalline chitin, regain much of this ability when combined with a lytic polysaccharide monooxygenase (LPMO). When combined with an LPMO, several less processive chitinase mutants showed equal or even increased activity on chitin compared to the wild-type. Thus, LPMOs affect the need for processivity in polysaccharide degrading enzyme cocktails, which implies that the composition of such cocktails may need reconsideration.en_US
dc.language.isoengen_US
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/deed.no*
dc.titleTreatment of recalcitrant crystalline polysaccharides with lytic polysaccharide monooxygenase relieves the need for glycoside hydrolase processivityen_US
dc.typePeer revieweden_US
dc.typeJournal articleen_US
dc.description.versionacceptedVersionen_US
dc.source.journalCarbohydrate Researchen_US
dc.identifier.doi10.1016/j.carres.2019.01.001
dc.identifier.cristin1659241
dc.relation.projectNorges forskningsråd: 209335en_US
dc.relation.projectNorges forskningsråd: 262853en_US
cristin.unitcode192,12,0,0
cristin.unitnameKjemi, bioteknologi og matvitenskap
cristin.ispublishedtrue
cristin.fulltextpostprint
cristin.qualitycode1


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Attribution-NonCommercial-NoDerivatives 4.0 Internasjonal
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