Molecular cloning, expression and characterization of bile salt hydrolase from Lactobacillus rhamnosus E9 strain

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dc.authorid0000-0002-2666-6383en_US
dc.authorid0000-0002-7050-4082
dc.authorid0000-0001-6906-5257
dc.contributor.authorKaya, Yeşim
dc.contributor.authorKök, Mehmet Şamil
dc.contributor.authorÖztürk, Mehmet
dc.date.accessioned2021-06-23T19:49:12Z
dc.date.available2021-06-23T19:49:12Z
dc.date.issued2017
dc.departmentBAİBÜ, Mühendislik Fakültesi, Gıda Mühendisliği Bölümüen_US
dc.description.abstractBile salt hydrolase (BSH) enzyme, commonly found in probiotic bacteria of gut origin, catalyzes the hydrolysis of glycine and/or taurine-conjugated bile salts allowing for colonization of the bacteria in the gut and contributing to a decrease in levels of cholesterol. However an excessive deconjugation of tauro-conjugated bile salts and production of secondary bile acid can have harmful side-effects. The aim of this study was to characterize the activity of BSH enzymes from Lactobacillus rhamnosus E9, a popular probiotic strain. The bsh gene was cloned, expressed, purified and characterized in Escherichia coli BLR(DE3) strain. The hydrolysis activities and substrate specificities of the recombinant BSH (rBSH) enzyme were examined using six different bile acids. Nucleotide sequence analysis results indicated that the bsh of E9 contained an open reading frame (ORF) of 1014 and nucleotides encoding a 338-amino acid protein with a molecular weight of 37 kDa. Five catalytically important amino acids and the amino acid motifs located around the active site were highly conserved. The rBSH showed a slight preference towards glycine-conjugated to tauro-conjugated bile salts. This confirms that it is a safe strain for probiotics and its preference for glycine-conjugated bile salts should be further investigated.en_US
dc.identifier.doi10.1080/08905436.2017.1303778
dc.identifier.endpage140en_US
dc.identifier.issn0890-5436
dc.identifier.issn1532-4249
dc.identifier.issue2en_US
dc.identifier.scopus2-s2.0-85019060404en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage128en_US
dc.identifier.urihttps://doi.org/10.1080/08905436.2017.1303778
dc.identifier.urihttps://hdl.handle.net/20.500.12491/9413
dc.identifier.volume31en_US
dc.identifier.wosWOS:000400939500005en_US
dc.identifier.wosqualityQ4en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.institutionauthorKök, Mehmet Şamil
dc.institutionauthorÖztürk, Mehmet
dc.language.isoenen_US
dc.publisherTaylor & Francis Incen_US
dc.relation.ispartofFood Biotechnologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectLactic Acid Bacteriaen_US
dc.subjectLactobacillus Rhamnosusen_US
dc.subjectProbioticsen_US
dc.subjectEnzyme Processingen_US
dc.subjectBile Salt Hydrolaseen_US
dc.subjectConjugated Bile Saltsen_US
dc.subjectSubstrate Specificityen_US
dc.titleMolecular cloning, expression and characterization of bile salt hydrolase from Lactobacillus rhamnosus E9 strainen_US
dc.typeArticleen_US

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