Characterization of a novel AA3_1 xylooligosaccharide dehydrogenase from Thermothelomyces myriococcoides CBS 398.93

dc.contributorAalto Universityen
dc.contributor.authorZhao, Hongboen_US
dc.contributor.authorKarppi, Johannaen_US
dc.contributor.authorNguyen, Thi Truc Minhen_US
dc.contributor.authorBellemare, Annieen_US
dc.contributor.authorTsang, Adrianen_US
dc.contributor.authorMaster, Emmaen_US
dc.contributor.authorTenkanen, Maijaen_US
dc.contributor.departmentDepartment of Bioproducts and Biosystemsen
dc.contributor.groupauthorProtein Technologyen
dc.contributor.organizationConcordia Universityen_US
dc.contributor.organizationUniversity of Helsinkien_US
dc.descriptionFunding Information: This work was conducted with the funding from Academy of Finland for COCOA (Project Codes 308996 and 308997), Novo Nordisk Foundation for BIOSEMBL and Finnish Cultural Foundation. Publisher Copyright: © 2022, The Author(s).
dc.description.abstractBackground: The Carbohydrate-Active enZymes (CAZy) auxiliary activity family 3 (AA3) comprises flavin adenine dinucleotide-dependent (FAD) oxidoreductases from the glucose–methanol–choline (GMC) family, which play auxiliary roles in lignocellulose conversion. The AA3 subfamily 1 predominantly consists of cellobiose dehydrogenases (CDHs) that typically comprise a dehydrogenase domain, a cytochrome domain, and a carbohydrate-binding module from family 1 (CBM1). Results: In this work, an AA3_1 gene from T. myriococcoides CBS 398.93 encoding only a GMC dehydrogenase domain was expressed in Aspergillus niger. Like previously characterized CDHs, this enzyme (TmXdhA) predominantly accepts linear saccharides with β-(1 → 4) linkage and targets the hydroxyl on the reducing anomeric carbon. TmXdhA was distinguished, however, by its preferential activity towards xylooligosaccharides over cellooligosaccharides. Amino acid sequence analysis showed that TmXdhA possesses a glutamine at the substrate-binding site rather than a threonine or serine that occupies this position in previously characterized CDHs, and structural models suggest the glutamine in TmXdhA could facilitate binding to pentose sugars. Conclusions: The biochemical analysis of TmXdhA revealed a catalytic preference for xylooligosaccharide substrates. The modeled structure of TmXdhA provides a reference for the screening of oxidoreductases targeting xylooligosaccharides. We anticipate TmXdhA to be a good candidate for the conversion of xylooligosaccharides to added-value chemicals by its exceptional catalytic ability.en
dc.description.versionPeer revieweden
dc.identifier.citationZhao, H, Karppi, J, Nguyen, T T M, Bellemare, A, Tsang, A, Master, E & Tenkanen, M 2022, ' Characterization of a novel AA3_1 xylooligosaccharide dehydrogenase from Thermothelomyces myriococcoides CBS 398.93 ', Biotechnology for Biofuels and Bioproducts, vol. 15, no. 1, 135 .
dc.identifier.otherPURE UUID: 17d19b5b-fcc1-4440-9ca5-93a794708596en_US
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dc.publisherBioMed Central
dc.relation.ispartofseriesBiotechnology for Biofuels and Bioproductsen
dc.relation.ispartofseriesVolume 15, issue 1en
dc.subject.keywordCAZy AA3en_US
dc.subject.keywordCellobiose dehydrogenaseen_US
dc.subject.keywordThermothelomyces myriococcoidesen_US
dc.subject.keywordXylooligosaccharide dehydrogenaseen_US
dc.titleCharacterization of a novel AA3_1 xylooligosaccharide dehydrogenase from Thermothelomyces myriococcoides CBS 398.93en
dc.typeA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessäfi