Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/10483
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dc.contributor.authorArslanoğlu, Alper-
dc.contributor.authorÇil, Çağlar-
dc.date.accessioned2021-01-24T18:44:54Z-
dc.date.available2021-01-24T18:44:54Z-
dc.date.issued2020-
dc.identifier.issn23222921-
dc.identifier.issn17283043-
dc.identifier.urihttps://doi.org/10.30498/IJB.2020.141895.2343-
dc.identifier.urihttps://hdl.handle.net/11147/10483-
dc.description.abstractBackground: Lipases secreted front various Rhizopus oryzae strains were previously expressed in Escherichia coli, Pichia pastoris, and Saccharomyces cerevisiae and was shown to have distinct activities in response to different temperatures, metal ions, organic solvents, and specific substrates. However, until now, no other research biochemically characterized the functions of extracellular pro-lipase in a novel Rhizopus oryzae KU45. Objectives: Characterization of a novel extracellular lipase front fungus R. orvzae KU45 after heterologous expression in E. coli BL21 (DE3) strain. Materials and Methods: An extracellular lipase producing fungus was isolated from a soil sample and identified as a strain of R. oryzae by partial 18S rRNA gene sequencing. It was named as R. oryzae KU45. The lipase gene of KU45 was cloned into pET-28a expression vector and expressed in E. coli as inclusion bodies. The recombinant lipase was purified, refolded and characterized. Results: The lipase exhibited maximum activity at 45 degrees C, at slightly alkaline pH. It showed a broad substrate specificity acting on p-nitrophenyl esters with C-8-C-16 acyl groups as substrates and, many of the organic solvents and metal ions tested did not have any adverse effects on the enzyme activity. Conclusions: High stability, broad substrate specificity and activity at mesophilic temperatures in the presence of organic solvents, and metal ions make the extracellular lipase of KU45 a candidate for various biotechnological applications.en_US
dc.description.sponsorshipState Planning Agency of TurkeyTurkiye Cumhuriyeti Kalkinma Bakanligien_US
dc.description.sponsorshipThis work was funded by the State Planning Agency of Turkey.en_US
dc.language.isoenen_US
dc.publisherNational Institute of Genetic Engineering and Biotechnologyen_US
dc.relation.ispartofIranian Journal of Biotechnologyen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectEscherichia colien_US
dc.subjectExtracellular lipaseen_US
dc.subjectEnzymeen_US
dc.subjectGene cloning and expressionen_US
dc.subjectInclusion bodyen_US
dc.subjectRhizopus oryzaeen_US
dc.titleGene Cloning, Heterologous Expression and Biochemical Characterization of a Novel Extracellular Lipase From Rhizopus Oryzae Ku45en_US
dc.typeArticleen_US
dc.institutionauthorArslanoğlu, Alper-
dc.institutionauthorÇil, Çağlar-
dc.departmentİzmir Institute of Technology. Molecular Biology and Geneticsen_US
dc.identifier.volume18en_US
dc.identifier.issue2en_US
dc.identifier.startpage47en_US
dc.identifier.endpage56en_US
dc.identifier.wosWOS:000574535600006en_US
dc.identifier.scopus2-s2.0-85102270862en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.30498/IJB.2020.141895.2343-
dc.identifier.pmid33542939en_US
dc.relation.doi10.30498/IJB.2020.141895.2343en_US
dc.coverage.doi10.30498/IJB.2020.141895.2343en_US
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.openairetypeArticle-
item.cerifentitytypePublications-
crisitem.author.dept04.03. Department of Molecular Biology and Genetics-
Appears in Collections: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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