Molecular cloning, characterization, and comparison of four bile salt hydrolase-related enzymes from lactobacillus plantarum GD2 of human origin

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dc.contributor.authorÖztürk, Mehmet
dc.contributor.authorAydın, Yasin
dc.contributor.authorKılıçsaymaz, Zekiye
dc.contributor.authorÖnal, Cansu
dc.contributor.authorBa, Ndeye
dc.date.accessioned2019-05-13T08:57:56Z
dc.date.available2019-05-13T08:57:56Z
dc.date.issued2018
dc.departmentHitit Üniversitesi, Fen Edebiyat Fakültesi, Biyoloji Bölümü
dc.description.abstractA bile salt hydrolase (bsh) enzyme deconjugate taurine and glycine-linked bile salts. Because of the strong implications between deconjugation of tauro- or gluco-conjugated salts and its positive or negative health consequences, the characterization of the bsh enzymes is important. bshs from different lactobacilli species, even strains, exhibit higher variation in sequence, kinetic properties, and substrate specificity. In the present study four bsh related genes from Lactobacillus plantarum GD2 strain were cloned and expressed in Escherichia coli BLR (DE3) strain. Amino acid residues of recombinant bshs were analyzed and their deconjugation abilities were tested with six human conjugated bile salts. Results indicated that the genetic distance among four related bsh genes in Lb. plantarum is far from each other and bsh2-4 enzymes share significant sequence homology specifically with penicillin V acylase (PVA) family members. Biochemical and the in silico analysis suggest that the bsh1 enzyme is a member of the bsh family while bsh2-4 enzymes are members of the PVA family. © 2018, © 2018 Taylor & Francis.
dc.identifier.citationÖztürk, M., Aydın, Y., Kılıçsaymaz, Z., Önal, C., Ba, N. (2018). Molecular cloning, characterization, and comparison of four bile salt hydrolase-related enzymes from lactobacillus plantarum GD2 of human origin. Food Biotechnology, 32(3), 191-205.
dc.identifier.doi10.1080/08905436.2018.1507911
dc.identifier.endpage205en_US
dc.identifier.issn0890-5436
dc.identifier.issue3en_US
dc.identifier.scopusqualityQ2
dc.identifier.startpage191en_US
dc.identifier.urihttps://doi.org/10.1080/08905436.2018.1507911
dc.identifier.urihttps://hdl.handle.net/11491/1037
dc.identifier.volume32en_US
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherTaylor and Francis Inc.
dc.relation.ispartofFood Biotechnology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectBile Salt Hydrolaseen_US
dc.subjectConjugated Bile Acidsen_US
dc.subjectLactobacillus Plantarumen_US
dc.subjectProbioticsen_US
dc.subjectSubstrate Specificityen_US
dc.titleMolecular cloning, characterization, and comparison of four bile salt hydrolase-related enzymes from lactobacillus plantarum GD2 of human origin
dc.typeArticle

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