Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/10376
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dc.contributor.authorBurhanoğlu, Tülintr
dc.contributor.authorSürmeli, Yusuftr
dc.contributor.authorŞanlı Mohamed, Gülşahtr
dc.date.accessioned2021-01-24T18:34:20Z-
dc.date.available2021-01-24T18:34:20Z-
dc.date.issued2020-
dc.identifier.issn0141-8130-
dc.identifier.issn1879-0003-
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2020.07.171-
dc.identifier.urihttps://hdl.handle.net/10376-
dc.description.abstractIn this study, the heterologous expression and biochemical characterization of a thermostable alpha-amylase from Geobacillus sp. GS33 was investigated. The recombinant alpha-amylase was overexpressed in Escherichia coli BL21 (lambda DE) and purified via anion exchange and size-exclusion chromatography. The purified alpha-amylase had a molecular weight of about 60 kDa, and was active in a broad range of pH 3-10 and temperature (40-90 degrees C) withmaximumactivity at pH 7-8 and 60 degrees C. The enzyme retained 50% residual activity at 65 degrees C, but only 20% at 85 degrees C after 16 h. At pH 9 and pH 7, the residual activity at 65 degrees C was 50% and 30%, respectively. The enzymewas remarkably activated by Co2+, Ca2+, Mg2+, PMSF, DTT, and Triton X-100, but partially inhibited by Cu2+, methanol, hexane, ethanol, acetone, SDS, and Tween 20. A molecular phylogeny analysis showed that the enzyme's amino acid sequence had the closest connection with an alpha-amylase from Geobacillus thermoleovorans subsp. stromboliensis nov. 3D-structure-based amino acid sequence alignments revealed that the three catalytic residues (D217, E246, D314) and the four Ca2+ ion coordination residues (N143, E177, D186, H221) were conserved in alpha-amylase from Geobacillus sp. GS33. The temperature stability and neutral pH optimum suggest that the enzyme may be useful for industrial applications. (C) 2020 Elsevier B.V. All rights reserved.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relation.ispartofInternational Journal of Biological Macromoleculesen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAlpha-Amylaseen_US
dc.subjectGeobacillus sp.en_US
dc.subjectThermostabilityen_US
dc.titleIdentification and characterization of novel thermostable alpha-amylase from Geobacillus sp. GS33en_US
dc.typeArticleen_US
dc.institutionauthorBurhanoğlu, Tülintr
dc.institutionauthorSürmeli, Yusuftr
dc.institutionauthorŞanlı Mohamed, Gülşahtr
dc.departmentİzmir Institute of Technology. Bioengineeringen_US
dc.departmentİzmir Institute of Technology. Chemistryen_US
dc.identifier.volume164en_US
dc.identifier.startpage578en_US
dc.identifier.endpage585en_US
dc.identifier.wosWOS:000588093700054en_US
dc.identifier.scopus2-s2.0-85088394880en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıtr
dc.identifier.doi10.1016/j.ijbiomac.2020.07.171-
dc.identifier.pmid32693140en_US
dc.relation.doi10.1016/j.ijbiomac.2020.07.171en_US
dc.coverage.doi10.1016/j.ijbiomac.2020.07.171en_US
dc.identifier.wosqualityQ1-
dc.identifier.scopusqualityQ1-
item.fulltextWith Fulltext-
item.openairetypeArticle-
item.cerifentitytypePublications-
item.grantfulltextopen-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.author.dept04.01. Department of Chemistry-
Appears in Collections: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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