Cloning, purification and characterization of a thermostable β- galactosidase from Bacillus licheniformis strain KG9

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dc.contributor.authorBekler, Fatma Matpan
dc.contributor.authorStougaard, Peter
dc.contributor.authorGüven, Kemal
dc.contributor.authorGüven, Reyhan Gül
dc.contributor.authorAcer, Ömer
dc.date.accessioned2024-04-24T17:56:41Z
dc.date.available2024-04-24T17:56:41Z
dc.date.issued2015
dc.departmentDicle Üniversitesi, Fen Fakültesi, Biyoloji Bölümüen_US
dc.description.abstractA thermo- and alkalitolerant Bacillus licheniformis KG9 isolated from Taslidere hot water spring in Batman/Turkey was found to produce a thermostable ?-galactosidase. Phylogenetic analysis showed that the 16S rRNA gene from B. licheniformis strain KG9 was 99.9% identical to that of the genome sequenced B. licheniformis strain DSM 13. Analysis of the B. licheniformis DSM 13 genomic sequence revealed four putative ?-galactosidase genes. PCR primers based on the genome sequence of strain DSM 13 were used to isolate the corresponding ?-galactosidase genes from B. licheniformis strain KG9. The calculated molecular weights of the ?-galactosidases I, II, III, and IV using sequencing data were 30, 79, 74, and 79 kDa, respectively. The genes were inserted into an expression vector and recombinant ?-galactosidase was produced in Escherichia coli. Of the four ?-galactosidase genes identified in strain KG9, three of them were expressed as active, intracellular enzymes in E. coli. One of the recombinant enzymes, ?-galactosidase III, was purified and characterized. Optimal temperature and pH was determined to be at 60 °C and pH 6.0, respectively. Km was determined to be 1.3 mM and 13.3 mM with oNPG (ortho-nitrophenyl-?-D-galactopyranoside) and lactose as substrates, respectively, and Vmax was measured to 1.96 ?mol/min and 1.55 ?mol/min with oNPG and lactose, respectively.en_US
dc.identifier.citationBekler, F. M., Stougaard, P., Güven, K., Güven, R. G. ve Acer, Ö. (2015). Cloning, purification and characterization of a thermostable β- galactosidase from Bacillus licheniformis strain KG9. Cellular and Molecular Biology, 61(3), 71-78.
dc.identifier.doi10.14715/cmb/2015.61.3.14
dc.identifier.endpage78en_US
dc.identifier.issn0145-5680
dc.identifier.issue3en_US
dc.identifier.pmid26115614
dc.identifier.scopus2-s2.0-84963701861
dc.identifier.scopusqualityQ4
dc.identifier.startpage71en_US
dc.identifier.urihttps://doi.org/10.14715/cmb/2015.61.3.14
dc.identifier.urihttps://hdl.handle.net/11468/23621
dc.identifier.volume61en_US
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoenen_US
dc.publisherCellular and Molecular Biology Associationen_US
dc.relation.ispartofCellular and Molecular Biology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBacillus licheniformisen_US
dc.subjectEnzyme activityen_US
dc.subjectPurificationen_US
dc.subjectRecombinant Dnaen_US
dc.subjectThermophilesen_US
dc.subject?-Galactosidaseen_US
dc.titleCloning, purification and characterization of a thermostable β- galactosidase from Bacillus licheniformis strain KG9en_US
dc.titleCloning, purification and characterization of a thermostable ?- galactosidase from Bacillus licheniformis strain KG9
dc.typeArticleen_US

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