Immobilization of lipase in organic solvent in the presence of fatty acid additives

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dc.contributor.authorOzturk, Taylan K.
dc.contributor.authorKilinc, Ali
dc.date.accessioned2019-10-27T21:29:19Z
dc.date.available2019-10-27T21:29:19Z
dc.date.issued2010
dc.departmentEge Üniversitesien_US
dc.description.abstractIn this study porcine pancreatic lipase (PPL) was covalently immobilized on cross-linked polyvinyl alcohol (PVA) in organic media in the presence of fatty acid additives in order to improve its immobilized activity. The effects of fatty acid additions to the immobilization media were investigated choosing tributyrin hydrolysis in water and ester synthesis by immobilized PPL in n-hexane. Various fatty acids which are also the substrates of lipases in esterification reactions were used as active site protecting agents during the immobilization process in an organic solvent. The obtained results showed that covalent immobilization carried out in the presence of fatty acids as protective ligands improved the hydrolytic and esterification activity of immobilized enzyme. A remarkable increase in activity of the immobilized PPL was obtained when octanoic acid was used as an additive and the hydrolytic activity was increased from 5.2 to 19.2 mu mol min(-1) mg(-1) as compared to the non-additive immobilization method. With the increase of hydrolytic activity of immobilized lipase in the presence of octanoic acid, in an analogous manner, the rate of esterification for the synthesis of butyl octanoate was also increased from 7.3 to 26.3 mu mol min(-1) g(-1) immobilized protein using controlled thermodynamic water activities with saturated salt solutions. In addition, the immobilized PPL activity was maintained at levels representing 63% of its original activity value after 5 repeated uses. The proposed method could be adopted for a wide variety of other enzymes which have highly soluble substrates in organic solvent such as other lipases and esterases. (C) 2010 Elsevier B.V. All rights reserved.en_US
dc.description.sponsorshipScientific Research Foundation of Ege University, Izmir, TurkeyEge University [Sci-2007-13]en_US
dc.description.sponsorshipWe thank the Scientific Research Foundation of Ege University, Izmir, Turkey (BAP-Grant Number Sci-2007-13) for financial support of this work.en_US
dc.identifier.doi10.1016/j.molcatb.2010.08.008
dc.identifier.endpage218en_US
dc.identifier.issn1381-1177
dc.identifier.issn1873-3158
dc.identifier.issn1381-1177en_US
dc.identifier.issn1873-3158en_US
dc.identifier.issue03.Apren_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.startpage214en_US
dc.identifier.urihttps://doi.org/10.1016/j.molcatb.2010.08.008
dc.identifier.urihttps://hdl.handle.net/11454/45269
dc.identifier.volume67en_US
dc.identifier.wosWOS:000284566200009en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherElsevier Science Bven_US
dc.relation.ispartofJournal of Molecular Catalysis B-Enzymaticen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectPorcine pancreatic lipaseen_US
dc.subjectImmobilization in organic solventen_US
dc.subjectAdditivesen_US
dc.subjectEsterificationen_US
dc.subjectWater activityen_US
dc.subjectFatty aciden_US
dc.titleImmobilization of lipase in organic solvent in the presence of fatty acid additivesen_US
dc.typeArticleen_US

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