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dc.contributor.authorJunghare, Madan
dc.contributor.authorManavalan, Tamilvendan
dc.contributor.authorFredriksen, Lasse
dc.contributor.authorLeiros, Ingar
dc.contributor.authorAltermark, Bjørn
dc.contributor.authorEijsink, Vincent
dc.contributor.authorVaaje-Kolstad, Gustav
dc.date.accessioned2023-08-30T08:29:33Z
dc.date.available2023-08-30T08:29:33Z
dc.date.issued2023-04-04
dc.description.abstractBackground Cellulases play a key role in the enzymatic conversion of plant cell-wall polysaccharides into simple and economically relevant sugars. Thus, the discovery of novel cellulases from exotic biological niches is of great interest as they may present properties that are valuable in the biorefning of lignocellulosic biomass. Results We have characterized a glycoside hydrolase 5 (GH5) domain of a bi-catalytic GH5-GH6 multi-domain enzyme from the unusual gill endosymbiont Teredinibacter waterburyi of the wood-digesting shipworm Psiloteredo megotara. The catalytic GH5 domain, was cloned and recombinantly produced with or without a C-terminal family 10 carbohydrate-binding module (CBM). Both variants showed hydrolytic endo-activity on soluble substrates such as β-glucan, carboxymethylcellulose and konjac glucomannan, respectively. However, low activity was observed towards the crystalline form of cellulose. Interestingly, when co-incubated with a cellulose-active LPMO, a clear syn‑ ergy was observed that boosted the overall hydrolysis of crystalline cellulose. The crystal structure of the GH5 catalytic domain was solved to 1.0 Å resolution and revealed a substrate binding cleft extension containing a putative+3 subsite, which is uncommon in this enzyme family. The enzyme was active in a wide range of pH, temperatures and showed high tolerance for NaCl. Conclusions This study provides significant knowledge in the discovery of new enzymes from shipworm gill endo‑ symbionts and sheds new light on biochemical and structural characterization of cellulolytic cellulase. Study demon‑ strated a boost in the hydrolytic activity of cellulase on crystalline cellulose when co-incubated with cellulose-active LPMO. These findings will be relevant for the development of future enzyme cocktails that may be useful for the biotechnological conversion of lignocellulose.en_US
dc.identifier.citationJunghare, Manavalan, Fredriksen, Leiros, Altermark, Eijsink, Vaaje-Kolstad. Biochemical and structural characterisation of a family GH5 cellulase from endosymbiont of shipworm P. megotara. Biotechnology for Biofuels and Bioproducts. 2023;16(1):1-15en_US
dc.identifier.cristinIDFRIDAID 2144242
dc.identifier.doi10.1186/s13068-023-02307-1
dc.identifier.issn2731-3654
dc.identifier.urihttps://hdl.handle.net/10037/30527
dc.language.isoengen_US
dc.publisherBMCen_US
dc.relation.journalBiotechnology for Biofuels and Bioproducts
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2023 The Author(s)en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0en_US
dc.rightsAttribution 4.0 International (CC BY 4.0)en_US
dc.titleBiochemical and structural characterisation of a family GH5 cellulase from endosymbiont of shipworm P. megotaraen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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Attribution 4.0 International (CC BY 4.0)
Except where otherwise noted, this item's license is described as Attribution 4.0 International (CC BY 4.0)