Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/12773
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dc.contributor.authorSürmeli, Yusuftr
dc.contributor.authorŞanlı Mohamed, Gülşahtr
dc.date.accessioned2023-01-19T06:54:30Z-
dc.date.available2023-01-19T06:54:30Z-
dc.date.issued2022-
dc.identifier.urihttps://doi.org/10.1002/bab.2423-
dc.identifier.urihttps://hdl.handle.net/11147/12773-
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.en_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.relation.ispartofBiotechnology and Applied Biochemistryen_US
dc.rightsinfo:eu-repo/semantics/embargoedAccessen_US
dc.subjectDirected evolutionen_US
dc.subjectError-prone PCR (epPCR)en_US
dc.subjectGeobacillus vulcanien_US
dc.titleStructural and functional analyses of GH51 alpha-L-arabinofuranosidase of Geobacillus vulcani GS90 reveal crucial residues for catalytic activity and thermostabilityen_US
dc.typeArticleen_US
dc.authorid0000-0003-0282-4428en_US
dc.authorid0000-0002-9645-6314en_US
dc.institutionauthorSürmeli, Yusuftr
dc.institutionauthorŞanlı Mohamed, Gülşahtr
dc.departmentİzmir Institute of Technology. Chemistryen_US
dc.departmentİzmir Institute of Technology. Bioengineeringen_US
dc.identifier.wosWOS:000898519400001en_US
dc.identifier.scopus2-s2.0-85144061522en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıtr
dc.identifier.doi10.1002/bab.2423-
dc.identifier.pmid36455188-
dc.relation.issn0885-4513en_US
dc.identifier.scopusqualityQ3-
item.fulltextWith Fulltext-
item.openairetypeArticle-
item.cerifentitytypePublications-
item.grantfulltextembargo_20251201-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.author.dept04.01. Department of Chemistry-
Appears in Collections:Bioengineering / Biyomühendislik
Chemistry / Kimya
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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