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Lipase from new isolate bacillus cereus ATA179: Optimization of production conditions, partial purification, characterization and its potential in the detergent industry

dc.contributor.authorDemirkan, Elif
dc.contributor.authorAybey Çetinkaya, Aynur
dc.contributor.authorAbdou, Maoulida
dc.contributor.buuauthorDEMİRKAN, ELİF
dc.contributor.buuauthorAybey Çetinkaya, Aynur
dc.contributor.buuauthorAbdou, Maoulida
dc.contributor.departmentBursa Uludağ Üniversitesi/Fen-Edebiyat Fakültesi/Biyoloji Bölümü
dc.contributor.orcid0000-0002-5292-9482
dc.contributor.orcid0000-0003-2743-9745
dc.contributor.researcheridABI-4472-2020
dc.contributor.researcheridCJN-1872-2022
dc.contributor.researcheridCAU-1487-2022
dc.date.accessioned2024-06-14T08:19:38Z
dc.date.available2024-06-14T08:19:38Z
dc.date.issued2021-01-01
dc.description.abstractIn this study, 341 Bacillus sp. strains were isolated from agricultural soils of Turkey. The potent extracellular lipase producer was selected. It was identified by 16S rRNA, named as Bacillus cereus ATA179. Optimal nutritional and physical parameters for lipase production were determined. Sucrose as the carbon source, (NHIHPO, as the nitrogen source, CaCl2 as the metal ion were obtained. The best results of physical parameters were stated at 45 degrees C, pH 7.0, shaking rate 50 rpm, inoculation amount 7% and inoculum age 24 h. ATA179 strain showed a 51% increase in enzyme production in the modified medium created by optimizing nutritional and physical conditions. Optimum pH value and temperature were found as 6.0 and 55 degrees C, respectively. CaCl2, Tween 20, Triton X-100 had an activating effect on enzyme activity. V-max and K-m kinetic values were found as 18.28 U/mL and 0.11 mM, respectively. The molecular weight was determined as 47 kDa. Lipase was found to be stable up to 75 days at -20 degrees C. The potential of the enzyme in detergent industry was also investigated. It was not affected by detergent additives, but was found to be effective in removing oils from contaminated fabrics. This new lipase may have potential to be used in detergent industry.
dc.identifier.doi10.3906/biy-2101-22
dc.identifier.eissn1303-6092
dc.identifier.endpage300
dc.identifier.issn1300-0152
dc.identifier.issue3
dc.identifier.startpage287
dc.identifier.urihttps://doi.org/10.3906/biy-2101-22
dc.identifier.urihttps://journals.tubitak.gov.tr/biology/vol45/iss3/5/
dc.identifier.urihttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8313942/
dc.identifier.urihttps://hdl.handle.net/11452/42202
dc.identifier.volume45
dc.identifier.wos000667755700005
dc.indexed.wosWOS.SCI
dc.language.isoen
dc.publisherTübitak Bilimsel ve Teknolojik Araştırma Kurumu
dc.relation.bapKUAP(F) 2018/5
dc.relation.journalTürk Biyoloji Dergisi
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectThermostable lipase
dc.subjectExtracellular lipase
dc.subjectParameters
dc.subjectCoagulans
dc.subjectAlignment
dc.subjectCulture
dc.subjectDesign
dc.subjectContaminated fabric
dc.subjectEnzyme
dc.subjectEnzymatic properties
dc.subjectScreening
dc.subjectTributyrin assay
dc.subjectScience & technology
dc.subjectLife sciences & biomedicine
dc.subjectBiology
dc.titleLipase from new isolate bacillus cereus ATA179: Optimization of production conditions, partial purification, characterization and its potential in the detergent industry
dc.typeArticle
dspace.entity.typePublication
relation.isAuthorOfPublication13b5deac-f120-4c0e-a42a-e8a47c700511
relation.isAuthorOfPublication.latestForDiscovery13b5deac-f120-4c0e-a42a-e8a47c700511

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