Site-directed mutagenesis of bile salt hydrolase (BSH) from lactobacillus plantarum B14 confirms the importance of the V58 and Y65 amino acids for activity and substrate specificity

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dc.authorid0000-0001-6906-5257en_US
dc.authorid0000-0003-2928-2577en_US
dc.authorid0000-0003-2701-3250en_US
dc.contributor.authorÖztürk, Mehmet
dc.contributor.authorKılıçsaymaz, Zekiye
dc.contributor.authorÖnal, Cansu
dc.date.accessioned2023-11-29T08:33:01Z
dc.date.available2023-11-29T08:33:01Z
dc.date.issued2023en_US
dc.departmentBAİBÜ, Fen Edebiyat Fakültesi, Biyoloji Bölümüen_US
dc.descriptionTBAG-116Z120 research grant from The Scientific Technological Research Council of Turkey (TUBITAK) has been received by Mehmet Ozturk.en_US
dc.description.abstractThe bile acids (BAs) de-conjugation is catalyzed by bile salt hydrolase (BSH) enzyme, that is an intestinal bacterial product and a member of the cholylglycine hydrolase (CGH) family. De-conjugated BAs alter BA-mediated signaling pathways such as glucose metabolism, energy homeostasis and lipid absorption and this makes the BSH clinically important. However, BSHs from different sources have a variable substrate preference to eight different bile salts. Although BSH is a well-studied enzyme, its molecular investigations based on BSH substrate recognition are not very well known. In this study, the relationship between substrate specificity of BSH from Lactobacillus plantarum B14 (LpBSH) and its loop II, the aliphatic-hydrophobic V58 and aromatic-hydrophobic Y65 residues in this loop was mutated and analyzed. While PCR-based site-directed mutagenesis was used to substitute V58 and Y65 amino acids for N58, F58, M58, C65, F65 and L65 amino acids, respectively, the BLR (DE3) strain of E. coli was used to express mutant recombinant LpBSHs (mrLpBSHs). Site-directed mutagenesis of LpBSH showed reduced activity of mrLpBSHs against six different BAs. Our results indicated that the V58 and mostly Y65 residues in loop II might be critical for the structural site that is involved in substrate specificity and catalysis. These findings suggested that V58 and Y65 residues of LpBSH might participate in substrate specificity and BSH substrate specificity may be dependent upon the collate group, rather than amino acid moieties. However, more mutagenesis-based investigation on other CGH family members are needed in order to understand the structure and substrate specificity relations of BSHs.en_US
dc.description.sponsorshipScientific Technological Research Council of Turkey (TUBITAK) [TBAG-116Z120]en_US
dc.identifier.citationÖztürk, M., Kılıçsaymaz, Z., & Önal, C. (2023). Site-Directed Mutagenesis of Bile Salt Hydrolase (BSH) from Lactobacillus plantarum B14 Confirms the Importance of the V58 and Y65 Amino Acids for Activity and Substrate Specificity. Food Biotechnology, 37(1), 74-88.en_US
dc.identifier.doi10.1080/08905436.2022.2164299
dc.identifier.endpage88en_US
dc.identifier.issn0890-5436
dc.identifier.issn1532-4249
dc.identifier.issue1en_US
dc.identifier.scopus2-s2.0-85147324583en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage74en_US
dc.identifier.urihttp://dx.doi.org/10.1080/08905436.2022.2164299
dc.identifier.urihttps://hdl.handle.net/20.500.12491/11890
dc.identifier.volume37en_US
dc.identifier.wosWOS:000925040600005en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.institutionauthorÖztürk, Mehmet
dc.institutionauthorKılıçsaymaz, Zekiye
dc.institutionauthorÖnal, Cansu
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.relation.tubitak[TBAG-116Z120]
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectLactobacillus Plantarum B14en_US
dc.subjectCatalytic Activityen_US
dc.subjectBile Salt Hydrolaseen_US
dc.subjectMolecular-Cloningen_US
dc.subjectFunctional-Analysisen_US
dc.subjectExpressionen_US
dc.titleSite-directed mutagenesis of bile salt hydrolase (BSH) from lactobacillus plantarum B14 confirms the importance of the V58 and Y65 amino acids for activity and substrate specificityen_US
dc.typeArticleen_US

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