Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/3598
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dc.contributor.advisorArslanoğlu, Alperen
dc.contributor.authorKarakaş, Fulya-
dc.date.accessioned2014-07-22T13:51:55Z-
dc.date.available2014-07-22T13:51:55Z-
dc.date.issued2013-03en
dc.identifier.urihttp://hdl.handle.net/11147/3598-
dc.descriptionThesis (Master)--Izmir Institute of Technology, Biotechnology, Izmir, 2013en
dc.descriptionIncludes bibliographical references (leaves. 27-31)en
dc.descriptionText in English; Abstract: Turkish and Englishen
dc.descriptionix, 33 leavesen
dc.descriptionFull text release delayed at author's request until 2015.05.02en
dc.description.abstractLipases are serine hydrolases that catalyze both the hydrolysis and synthesis of insoluble or poorly soluble long-chain triacylglycerols with an acyl chain length ≥ 10 carbon atoms based on the presence or absence of water. Lipases are produced and secreted by all kingdoms of life that are eukaryotes including plants, animals, fungi and prokaryotes including bacteria and archaea. However, microbial lipases, especially from bacteria, more useful than their plant and animal derivatives because of several important properties. Because of their acitivities in both aqueous and nonaqueous environments, lipases have specific applications in industry and medicine. The primary goals of this thesis were to clone and express the extra-cellular lipase gene from Pseudomonas sp. KE38, isolated from soil samples of Erciyes mountain in Kayseri, in E. coli and partial purification of the gene product. To achieve this aim, genome walking technique was used to obtain lipase gene from Pseudomonas sp. KE38, that gene was then cloned into pET28a expression vector and expressed in E. coli. The lipase expression of E. coli BL21 and its activity was screened with olive oil-Rhodamin B plate assay. After expression recombinant lipase was partially purified via inclusion body isolation. Moreover the optimum lipase production time of E. coli BL21 cells were determined and analyzed with SDS-PAGE. According to SDS-PAGE analysis the recombinant lipase was approximately 64 kDa and lipase production reached to the highest level after two hours of IPTG induction. As conclusion, recombinant lipase from Pseudomonas sp. KE38 was cloned into E. coli, expressed and partially purified.en
dc.language.isoenen_US
dc.publisherIzmir Institute of Technologyen
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subject.lcshLipase--Biotechnologyen
dc.subject.lcshMolecular cloningen
dc.subject.lcshEscherichia colien
dc.subject.lcshPseudomonasen
dc.titleCloning and expression of the pseudomonas KE38 extra-cellular lipase gene in E. colien_US
dc.typeMaster Thesisen_US
dc.institutionauthorKarakaş, Fulya-
dc.departmentThesis (Master)--İzmir Institute of Technology, Bioengineeringen_US
dc.relation.publicationcategoryTezen_US
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.grantfulltextopen-
item.fulltextWith Fulltext-
item.openairetypeMaster Thesis-
Appears in Collections:Master Degree / Yüksek Lisans Tezleri
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