Covalent immobilization of benzoylformate decarboxylase from Pseudomonas putida on magnetic epoxy support and its carboligation reactivity

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dc.contributor.authorTural, Bilsen
dc.contributor.authorTarhan, Tuba
dc.contributor.authorTural, Servet
dc.date.accessioned2024-04-24T16:15:32Z
dc.date.available2024-04-24T16:15:32Z
dc.date.issued2014
dc.departmentDicle Üniversitesien_US
dc.description.abstractEpoxy attached magnetic nanoparticles were prepared and used as solid support for covalent immobilization and stabilization of benzoylformate decarboxylase (BFD, E.C. 4.1.1.7) from Pseudomonas putida. A three-step immobilization/stabilization procedure is applied. The enzyme is firstly covalently immobilized under mild experimental conditions (e.g. pH 7.0, no added MgSO4 and 20 degrees C). Secondly, the enzyme is immobilized under more drastic conditions (higher pH values, higher ionic strengths, etc.) to facilitate an increase in effective concentration of the enzyme on the support near the epoxide reactive sites. Thirdly, the remaining epoxy groups are blocked to stop any additional interaction between the enzyme and the support. With more drastic conditions, the loading of enzyme can be increased from 1.25 to 6.70 mg enzyme per gram of support. The covalently bounded enzyme was characterized in terms of its activity and stability for the formation of (S)-2-hydroxypropiophenone (2-HPP). The activity of the immobilized BED was determined to be 53.0% related to the activity of the free enzyme. The immobilized biocatalyst retained 95% of its original activity after five reaction cycles. (C) 2014 Elsevier B.V. All rights reserved.en_US
dc.description.sponsorshipDicle University Research Fund (DUBAP) [13-ZEF-28]; Scientific and Technological Research Council of Turkey (TUBITAK) [109T497, COST Action CM0701]en_US
dc.description.sponsorshipThis project is funded by the financial support from Dicle University Research Fund (DUBAP, Project No. 13-ZEF-28) and the Scientific and Technological Research Council of Turkey (TUBITAK, 109T497), COST Action CM0701.en_US
dc.identifier.doi10.1016/j.molcatb.2014.02.016
dc.identifier.endpage194en_US
dc.identifier.issn1381-1177
dc.identifier.issn1873-3158
dc.identifier.scopus2-s2.0-84896338045
dc.identifier.scopusqualityN/A
dc.identifier.startpage188en_US
dc.identifier.urihttps://doi.org/10.1016/j.molcatb.2014.02.016
dc.identifier.urihttps://hdl.handle.net/11468/15843
dc.identifier.volume102en_US
dc.identifier.wosWOS:000335872900027
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoenen_US
dc.publisherElsevier Science Bven_US
dc.relation.ispartofJournal of Molecular Catalysis B-Enzymatic
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBenzoylformate Decarboxylaseen_US
dc.subjectCovalent Immobilizationen_US
dc.subjectMagnetic Epoxy Supporten_US
dc.subjectCarboligation Reactivityen_US
dc.titleCovalent immobilization of benzoylformate decarboxylase from Pseudomonas putida on magnetic epoxy support and its carboligation reactivityen_US
dc.titleCovalent immobilization of benzoylformate decarboxylase from Pseudomonas putida on magnetic epoxy support and its carboligation reactivity
dc.typeArticleen_US

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