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https://hdl.handle.net/11147/10483
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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Arslanoğlu, Alper | - |
dc.contributor.author | Çil, Çağlar | - |
dc.date.accessioned | 2021-01-24T18:44:54Z | - |
dc.date.available | 2021-01-24T18:44:54Z | - |
dc.date.issued | 2020 | - |
dc.identifier.issn | 23222921 | - |
dc.identifier.issn | 17283043 | - |
dc.identifier.uri | https://doi.org/10.30498/IJB.2020.141895.2343 | - |
dc.identifier.uri | https://hdl.handle.net/11147/10483 | - |
dc.description.abstract | Background: 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.sponsorship | State Planning Agency of TurkeyTurkiye Cumhuriyeti Kalkinma Bakanligi | en_US |
dc.description.sponsorship | This work was funded by the State Planning Agency of Turkey. | en_US |
dc.language.iso | en | en_US |
dc.publisher | National Institute of Genetic Engineering and Biotechnology | en_US |
dc.relation.ispartof | Iranian Journal of Biotechnology | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Escherichia coli | en_US |
dc.subject | Extracellular lipase | en_US |
dc.subject | Enzyme | en_US |
dc.subject | Gene cloning and expression | en_US |
dc.subject | Inclusion body | en_US |
dc.subject | Rhizopus oryzae | en_US |
dc.title | Gene Cloning, Heterologous Expression and Biochemical Characterization of a Novel Extracellular Lipase From Rhizopus Oryzae Ku45 | en_US |
dc.type | Article | en_US |
dc.institutionauthor | Arslanoğlu, Alper | - |
dc.institutionauthor | Çil, Çağlar | - |
dc.department | İzmir Institute of Technology. Molecular Biology and Genetics | en_US |
dc.identifier.volume | 18 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.startpage | 47 | en_US |
dc.identifier.endpage | 56 | en_US |
dc.identifier.wos | WOS:000574535600006 | en_US |
dc.identifier.scopus | 2-s2.0-85102270862 | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.identifier.doi | 10.30498/IJB.2020.141895.2343 | - |
dc.identifier.pmid | 33542939 | en_US |
dc.relation.doi | 10.30498/IJB.2020.141895.2343 | en_US |
dc.coverage.doi | 10.30498/IJB.2020.141895.2343 | en_US |
item.languageiso639-1 | en | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
item.grantfulltext | none | - |
item.openairetype | Article | - |
item.cerifentitytype | Publications | - |
crisitem.author.dept | 04.03. 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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