dc.contributor.author | Kaya, Yesim | |
dc.contributor.author | Kok, M. Samil | |
dc.contributor.author | Öztürk, Mehmet | |
dc.date.accessioned | 2020-11-20T14:54:50Z | |
dc.date.available | 2020-11-20T14:54:50Z | |
dc.date.issued | 2017 | |
dc.identifier.issn | 0890-5436 | |
dc.identifier.issn | 1532-4249 | |
dc.identifier.uri | https://doi.org/10.1080/08905436.2017.1303778 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12809/2180 | |
dc.description | Kaya, Yesim/0000-0002-2666-6383 | en_US |
dc.description | WOS: 000400939500005 | en_US |
dc.description.abstract | Bile 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.description.sponsorship | Abant Izzet Baysal UniversityAbant Izzet Baysal University [2012.03.01.560] | en_US |
dc.description.sponsorship | This work was supported by Scientific Research Projects of Abant Izzet Baysal University (2012.03.01.560). | en_US |
dc.item-language.iso | eng | en_US |
dc.publisher | Taylor & Francis Inc | en_US |
dc.item-rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Lactic Acid Bacteria | en_US |
dc.subject | Lactobacillus Rhamnosus | en_US |
dc.subject | Probiotics | en_US |
dc.subject | Enzyme Processing | en_US |
dc.subject | Bile Salt Hydrolase | en_US |
dc.subject | Conjugated Bile Salts | en_US |
dc.subject | Substrate Specificity | en_US |
dc.title | Molecular cloning, expression and characterization of bile salt hydrolase from Lactobacillus rhamnosus E9 strain | en_US |
dc.item-type | article | en_US |
dc.contributor.department | MÜ | en_US |
dc.contributor.departmentTemp | [Kaya, Yesim] Mugla Sitki Kocman Univ, Dept Mol Biol & Genet, Fac Sci, Mugla, Turkey -- [Kok, M. Samil] Abant Izzet Baysal Univ, Fac Engn & Architecture, Dept Food Engn, Bolu, Turkey -- [Ozturk, Mehmet] Abant Izzet Baysal Univ, Fac Arts & Sci, Dept Biol, Bolu, Turkey | en_US |
dc.identifier.doi | 10.1080/08905436.2017.1303778 | |
dc.identifier.volume | 31 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.startpage | 128 | en_US |
dc.identifier.endpage | 140 | en_US |
dc.relation.journal | Food Biotechnology | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |