Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/4027
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dc.contributor.advisorArslanoğlu, Alperen
dc.contributor.authorAdan, Aysun-
dc.date.accessioned2014-07-22T13:53:01Z-
dc.date.available2014-07-22T13:53:01Z-
dc.date.issued2009en
dc.identifier.urihttp://hdl.handle.net/11147/4027-
dc.descriptionThesis (Master)--Izmir Institute of Technology, Molecular Biology and Genetics, Izmir, 2009en
dc.descriptionIncludes bibliographical references (leaves: 46-49)en
dc.descriptionText in English; Abstract: Turkish and Englishen
dc.descriptionxii, 53 leavesen
dc.description.abstractLipases are serine hydrolases and catalyze both the hydrolysis and synthesis of long-chain triacylglycerols. Lipases have great importance since their wide usage in industry. Lipases are produced by microorganisms (bacteria and fungi), plants and animals. However, microbial lipases, especially from bacteria, more useful than their plant and animal derivatives because of several important properties. The primary goals of this thesis were to isolate and identify a lipase producing bacterium from soil sample from Erciyes mountain in Kayseri by 16S rRNA sequence analysis, find the sequence of lipase gene by degenerate PCR and inverse PCR and analyze of lipase gene for some important features like active site residues. The other purposes of this study were determination of lipase production conditions like optimum production time, partial purification and characterization of native lipase enzyme. Purification was performed by ammonium sulfate precipitation and gel filtration. Spectrophotometric lipase assay was used for enzyme characterization. As conclusion, a lipase producer bacterium was isolated from soil using rhodamine B-olive oil plate assay and identified as a strain of Pseudomonas fluorescens based on 16S rRNA sequence homology. Its partial lipase gene was obtained and it was suggested that the lipase belong to group 3 Pseudomonas lipases according to gene and amino acid homology search. Moreover, native lipase partially purified and characterized. The molecular mass of purified lipase was estimated to be approximately 43 kDa by SDS-PAGE. The optimum temperature and pH for the lipase were found to 45°C and pH 8, respectively.en
dc.language.isoenen_US
dc.publisherIzmir Institute of Technologyen
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subject.lccQP609.L5 A22 2009en
dc.subject.lcshLipase--Laboratory manualsen
dc.subject.lcshPsychrotrophic organismsen
dc.titleIsolation and identification of a lipase producing psychrotrophic bacteria from soil: Cloning and partial characterization of its lipaseen_US
dc.typeMaster Thesisen_US
dc.institutionauthorAdan, Aysun-
dc.departmentIzmir Institute of Technology. Molecular Biology and Geneticsen
dc.relation.publicationcategoryTezen_US
item.cerifentitytypePublications-
item.grantfulltextopen-
item.openairetypeMaster Thesis-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.languageiso639-1en-
item.fulltextWith Fulltext-
crisitem.author.dept04.03. Department of Molecular Biology and Genetics-
Appears in Collections:Master Degree / Yüksek Lisans Tezleri
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