Effects of structural changes in bile salt hydrolase enzyme on biocatalytic efficiency and activation energy at working pH and temperature conditions

dc.authorid0000-0002-0159-5283en_US
dc.authorid0000-0001-6906-5257en_US
dc.authorid0000-0003-2701-3250en_US
dc.authorid0000-0003-2928-2577en_US
dc.contributor.authorErmurat, Yakup
dc.contributor.authorÖztürk, Mehmet
dc.contributor.authorÖnal, Cansu
dc.contributor.authorKılıçsaymaz, Zekiye
dc.date.accessioned2023-11-15T10:47:32Z
dc.date.available2023-11-15T10:47:32Z
dc.date.issued2022en_US
dc.departmentBAİBÜ, Mühendislik Fakültesi, Çevre Mühendisliği Bölümüen_US
dc.descriptionThis work was supported by grants from the Scientific Research Project Office (number 2018.09.02.1271) of Bolu Abant Izzet Baysal University, Turkey.en_US
dc.description.abstractMicrobial bile salt hydrolases (BSHs) catalyse the hydrolysis of glycine and taurine-linked bile salts in the small intestine of humans. Achieving the effects of structural changes in BSH molecules on biocatalytic efficiency (kcat/Km) and activation energy (Ea) is necessary to determine biocatalytic performances of the enzymes. Amino acids responsible for biocatalytic activity or substrate specificity in BSH molecules were modified to determine the effects of structural changes on kcat/Km values and Ea values of the bioconversion reactions. Purified wild type positive control enzyme (pCON2) and mutant recombinant target enzymes (F18L and Y24L) reacted with six conjugated pure bile salt substrates at working temperature and pH conditions. The results of the hydrolysis conversion analysis conducted at various pH conditions were used to estimate kcat/Km, and the assays conducted at various temperature conditions were used to approximate Ea of the biocatalytic reactions. The quantified kcat/ Km value was found remarkably highest with mutant recombinant enzymes (Y24L), while the efficiency value with wild type (pCON2) was determined as lowest, indicating that the structural modifications in BSH molecules showed higher values. The alterations with the mutant-type enzymes F18L and Y24L resulted in decreasing kcat/Km and increasing Ea estimations of the hydrolysis conversion reactions.en_US
dc.description.sponsorshipScientific Research Project Office of Bolu Abant Izzet Baysal University, Turkey [2018.09.02.1271]en_US
dc.identifier.citationErmurat, Y., Öztürk, M., Önal, C., & Kılıçsaymaz, Z. (2022). Effects of Structural Changes in Bile Salt Hydrolase Enzyme on Biocatalytic Efficiency and Activation Energy at Working pH and Temperature Conditions. Kemija u industriji: Časopis kemičara i kemijskih inženjera Hrvatske, 71(7-8), 413-419.en_US
dc.identifier.doi10.15255/KUI.2021.075
dc.identifier.endpage419en_US
dc.identifier.issn0022-9830
dc.identifier.issn1334-9090
dc.identifier.issue7-8en_US
dc.identifier.startpage413en_US
dc.identifier.urihttp://dx.doi.org/10.15255/KUI.2021.075
dc.identifier.urihttps://hdl.handle.net/20.500.12491/11835
dc.identifier.volume71en_US
dc.identifier.wosWOS:000834775700002en_US
dc.identifier.wosqualityN/Aen_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.institutionauthorErmurat, Yakup
dc.institutionauthorÖztürk, Mehmet
dc.institutionauthorÖnal, Cansu
dc.institutionauthorKılıçsaymaz, Zekiye
dc.language.isoenen_US
dc.publisherHrvatsko Drustvo Kemjijskih Inzenjera I Tehnologaen_US
dc.relation.ispartofKemija U Industriji-Journal of Chemists And Chemical Engineersen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectBile Salten_US
dc.subjectWild Hydrolaseen_US
dc.subjectRecombinant Hydrolaseen_US
dc.subjectBiocatalytic Efficiencyen_US
dc.subjectCatalytic Efficiencyen_US
dc.subjectLactobacillus-Plantarumen_US
dc.titleEffects of structural changes in bile salt hydrolase enzyme on biocatalytic efficiency and activation energy at working pH and temperature conditionsen_US
dc.typeArticleen_US

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