Comparison of the efficiency of concentrated soluble recombinant phospholipase D and natural phospholipase D enzymes

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dc.contributor.authorSakmanoglu, Asli
dc.contributor.authorErganis, Osman
dc.date.accessioned2020-03-26T19:23:25Z
dc.date.available2020-03-26T19:23:25Z
dc.date.issued2016
dc.departmentSelçuk Üniversitesien_US
dc.description.abstractPhospholipase D (PLD) is a major virulence determinant of Corynebacterium pseudotuberculosis. Various studies have focused on the expression of recombinant PLD (rPLD) enzyme in different Escherichia coli strains, but generally a high yield of insoluble protein was reported. The aims of this study were to express soluble rPLD by different methods in E. coli. The rPLD and natural PLD (dPLD) enzymes were concentrated using an ultramembrane cassette system after the efficiencies of these concentrated enzymes were compared. The rPLD enzyme was expressed in One Shot (R) BL21(DE3) E. coli when induced by IPTG in TY medium. Soluble dPLD and rPLD enzyme hemolytic activities were determined using the reverse CAMP test. The nucleotide sequence of the rPLD gene was 99.7% similar to the PLD gene of C. pseudotuberculosis in the NCBI GenBank Database; these differences in nucleotides resulted in a difference in two amino acids. The rPLD protein concentration and the titer of hemolytic activity were 23.1 mg/mL and 1/256, respectively. Similarities in the enzyme characteristics were detected between rPLD and dPLD enzymes. These findings indicate that a protocol would be useful for the enhanced production of soluble rPLD in E. coli and a membrane cassette system for concentration the recombinant protein.en_US
dc.description.sponsorshipCoordinatorship for Scientific Research Projects of Selcuk University [SUBAPK, Konya, Turkey] [11102016]en_US
dc.description.sponsorshipThis study was supported by the Coordinatorship for Scientific Research Projects of Selcuk University [SUBAPK (No: 11102016), Konya, Turkey]. This article originated from part of a PhD thesis. The research was approved by the Ethics Committee of the Faculty of Veterinary Medicine, Selcuk University, Konya, Turkey (Ethics Committee Decision No: 2011-035). The abstract was presented at the XI Veterinary Microbiology Congress 2014, Antalya, Turkey, and published in the proceedings book.en_US
dc.identifier.doi10.3906/vet-1602-61en_US
dc.identifier.endpage680en_US
dc.identifier.issn1300-0128en_US
dc.identifier.issue6en_US
dc.identifier.scopusqualityQ3en_US
dc.identifier.startpage675en_US
dc.identifier.urihttps://dx.doi.org/10.3906/vet-1602-61
dc.identifier.urihttps://hdl.handle.net/20.500.12395/33385
dc.identifier.volume40en_US
dc.identifier.wosWOS:000391716100001en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakTR-Dizinen_US
dc.language.isoenen_US
dc.publisherSCIENTIFIC TECHNICAL RESEARCH COUNCIL TURKEY-TUBITAKen_US
dc.relation.ispartofTURKISH JOURNAL OF VETERINARY & ANIMAL SCIENCESen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.selcuk20240510_oaigen_US
dc.subjectEnzymeen_US
dc.subjectEscherichia colien_US
dc.subjectgenome analysisen_US
dc.subjectmicrobial protein synthesisen_US
dc.subjectsheepen_US
dc.titleComparison of the efficiency of concentrated soluble recombinant phospholipase D and natural phospholipase D enzymesen_US
dc.typeArticleen_US

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