Structural and functional analyses of GH51 alpha-L-arabinofuranosidase of Geobacillus vulcani GS90 reveal crucial residues for catalytic activity and thermostability

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dc.authorscopusid55758999000
dc.authorscopusid36680469600
dc.contributor.authorSürmeli, Yusuf
dc.contributor.authorSanli-Mohamed, Gülşah
dc.date.accessioned2023-05-06T17:23:41Z
dc.date.available2023-05-06T17:23:41Z
dc.date.issued2022
dc.departmentFakülteler, Ziraat Fakültesi, Tarımsal Biyoteknoloji Bölümü
dc.description.abstractAlpha-L-arabinofuranosidase (Abf) is of big interest in various industrial areas. Directed evolution is a powerful strategy to identify significant residues underlying Abf properties. Here, six active variants from GH51 Abf of Geobacillus vulcani GS90 (GvAbf) by directed evolution were overproduced, extracted, and analyzed at biochemical and structural levels. According to the activity and thermostability results, the most-active and the least-active variants were found as GvAbf51 and GvAbf52, respectively. GvAbf63 variant was more active than parent GvAbf by 20% and less active than GvAbf51. Also, the highest thermostability belonged to GvAbf52 with 80% residual activity after 1 h. Comparative sequence and structure analyses revealed that GvAbf51 possessed L307S displacement. Thus, this study suggested that L307 residue may be critical for GvAbf activity. GvAbf63 had H30D, Q90H, and L307S displacements, and H30 was covalently bound to E29 catalytic residue. Thus, H30D may decrease the positive effect of L307S on GvAbf63 activity, preventing E29 action. Besides, GvAbf52 possessed S215N, L307S, H473P, and G476C substitutions and S215 was close to E175 (acid–base residue). S215N may partially disrupt E175 action. Overall effect of all substitutions in GvAbf52 may result in the formation of the C–C bond between C171 and C213 by becoming closer to each other. © 2022 International Union of Biochemistry and Molecular Biology, Inc.
dc.identifier.doi10.1002/bab.2423
dc.identifier.issn0885-4513
dc.identifier.pmid36455188
dc.identifier.scopus2-s2.0-85144061522
dc.identifier.scopusqualityQ3
dc.identifier.urihttps://doi.org/10.1002/bab.2423
dc.identifier.urihttps://hdl.handle.net/20.500.11776/12241
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorSürmeli, Yusuf
dc.language.isoen
dc.publisherJohn Wiley and Sons Inc
dc.relation.ispartofBiotechnology and Applied Biochemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectdirected evolution
dc.subjecterror-prone PCR (epPCR)
dc.subjectGeobacillus vulcani
dc.subjectGH51 family
dc.subject?-L-arabinofuranosidase
dc.subjectStability
dc.subjectArabinofuranosidase
dc.subjectBiochemical level
dc.subjectDirected evolution
dc.subjectError prone PCR
dc.subjectError-prone PCR
dc.subjectGeobacillus vulcani
dc.subjectGh51 family
dc.subjectIndustrial area
dc.subjectProperty
dc.subject?-L-arabinofuranosidase
dc.subjectCatalyst activity
dc.titleStructural and functional analyses of GH51 alpha-L-arabinofuranosidase of Geobacillus vulcani GS90 reveal crucial residues for catalytic activity and thermostability
dc.typeArticle

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