Structural characterization of the family GH115 α-glucuronidase from Amphibacillus xylanus yields insight into its coordinated action with α-arabinofuranosidases

dc.contributorAalto-yliopistofi
dc.contributorAalto Universityen
dc.contributor.authorYan, Ruoyu
dc.contributor.authorWang, Weijun
dc.contributor.authorVuong, Thu V.
dc.contributor.authorXiu, Yang
dc.contributor.authorSkarina, Tatiana
dc.contributor.authorDi Leo, Rosa
dc.contributor.authorGatenholm, Paul
dc.contributor.authorToriz, Guillermo
dc.contributor.authorTenkanen, Maija
dc.contributor.authorStogios, Peter J.
dc.contributor.authorMaster, Emma R.
dc.contributor.departmentUniversity of Toronto
dc.contributor.departmentChalmers University of Technology
dc.contributor.departmentUniversidad de Guadalajara
dc.contributor.departmentUniversity of Helsinki
dc.contributor.departmentDepartment of Bioproducts and Biosystems
dc.date.accessioned2021-02-09T09:07:40Z
dc.date.available2021-02-09T09:07:40Z
dc.date.issued2021-05-25
dc.description| openaire: EC/H2020/648925/EU//BHIVE
dc.description.abstractThe coordinated action of carbohydrate-active enzymes has mainly been evaluated for the purpose of complete saccharification of plant biomass (lignocellulose) to sugars. By contrast, the coordinated action of accessory hemicellulases on xylan debranching and recovery is less well characterized. Here, the activity of two family GH115 α-glucuronidases (SdeAgu115A from Saccharophagus degradans, and AxyAgu115A from Amphibacillus xylanus) on spruce arabinoglucuronoxylan (AGX) was evaluated in combination with an α-arabinofuranosidase from families GH51 (AniAbf51A, aka E-AFASE from Aspergillus niger) and GH62 (SthAbf62A from Streptomyces thermoviolaceus). The α-arabinofuranosidases boosted (methyl)-glucuronic acid release by SdeAgu115A by approximately 50 % and 30 %, respectively. The impact of the α-arabinofuranosidases on AxyAgu115A activity was comparatively low, motivating its structural characterization. The crystal structure of AxyAgu115A revealed increased length and flexibility of the active site loop compared to SdeAgu115A. This structural difference could explain the ability of AxyAgu115A to accommodate more highly substituted arabinoglucuronoxylan, and inform enzyme selections for improved AGX recovery and use.en
dc.description.versionPeer revieweden
dc.format.extent8
dc.format.extent49-56
dc.format.mimetypeapplication/pdf
dc.identifier.citationYan , R , Wang , W , Vuong , T V , Xiu , Y , Skarina , T , Di Leo , R , Gatenholm , P , Toriz , G , Tenkanen , M , Stogios , P J & Master , E R 2021 , ' Structural characterization of the family GH115 α-glucuronidase from Amphibacillus xylanus yields insight into its coordinated action with α-arabinofuranosidases ' , NEW BIOTECHNOLOGY , vol. 62 , pp. 49-56 . https://doi.org/10.1016/j.nbt.2021.01.005en
dc.identifier.doi10.1016/j.nbt.2021.01.005
dc.identifier.issn1871-6784
dc.identifier.otherPURE UUID: dfb1ff09-027f-42eb-a11b-54c9d6e31554
dc.identifier.otherPURE ITEMURL: https://research.aalto.fi/en/publications/dfb1ff09-027f-42eb-a11b-54c9d6e31554
dc.identifier.otherPURE LINK: http://www.scopus.com/inward/record.url?scp=85100021533&partnerID=8YFLogxK
dc.identifier.otherPURE FILEURL: https://research.aalto.fi/files/55871151/1_s2.0_S1871678421000078_main.pdf
dc.identifier.urihttps://aaltodoc.aalto.fi/handle/123456789/102673
dc.identifier.urnURN:NBN:fi:aalto-202102091973
dc.language.isoenen
dc.publisherElsevier Science B.V.
dc.relationinfo:eu-repo/grantAgreement/EC/H2020/648925/EU//BHIVE
dc.relation.ispartofseriesNEW BIOTECHNOLOGYen
dc.relation.ispartofseriesVolume 62en
dc.rightsopenAccessen
dc.subject.keywordArabinoglucuronoxylan
dc.subject.keywordGH115
dc.subject.keywordGH51
dc.subject.keywordGH62
dc.subject.keywordHemicellulases
dc.subject.keywordα-Arabinofuranosidase
dc.subject.keywordα-Glucuronidase
dc.titleStructural characterization of the family GH115 α-glucuronidase from Amphibacillus xylanus yields insight into its coordinated action with α-arabinofuranosidasesen
dc.typeA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessäfi
dc.type.versionpublishedVersion
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