C18 Unsaturated Fatty Acid Selectivity of Lipases During the Acidolysis Reaction Between Tripalmitin and Oleic, Linoleic, and Linolenic Acids

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dc.authoridkarabulut, ihsan/0000-0002-9014-8863
dc.authoridHayaloglu, Ali Adnan/0000-0002-4274-2729
dc.authoridDurmaz, Gökhan/0000-0003-3423-8108
dc.authorwosidkarabulut, ihsan/ABG-7556-2020
dc.authorwosidHayaloglu, Ali Adnan/ABF-7063-2020
dc.authorwosidDurmaz, Gökhan/E-7121-2016
dc.contributor.authorKarabulut, Ihsan
dc.contributor.authorDurmaz, Gokhan
dc.contributor.authorHayaloglu, Ali Adnan
dc.date.accessioned2024-08-04T20:32:35Z
dc.date.available2024-08-04T20:32:35Z
dc.date.issued2010
dc.departmentİnönü Üniversitesien_US
dc.description.abstractThe C18 unsaturated fatty acid (UFA) selectivity of three immobilized lipases, namely, Lipozyme TL IM from Thermomyces lanuginosa, Lipozyme RM IM from Rhizomucor miehei, and Novozym 435 from Candida antarctica, was determined in acidolysis conducted in hexane. Tripalmitin with a mixture of equimolar quantities of C18 UFAs was used as the substrate. Significantly different incorporation rates were observed for C18 UFAs used (p < 0.05). The highest incorporation was obtained for all three C18 UFAs with Novozym 435 followed by Lipozyme RM IM and Lipozyme TL IM catalyzed acidolysis under default conditions (substrate mole ratio 1:1; temperature 50 A degrees C; reaction time 6 h; enzyme dosage 10%). Incorporation of the equimolar quantities of C18 UFAs was in the order C18:3 > C18:2 > C18:1 which also reflects C18 UFAs preferences of the lipases. The effects of operating variables on incorporation or UFA selectivity of lipases were also investigated. Among the experimental parameters including the mole ratio of fatty acid to triolein, temperature, enzyme dosage, and time on incorporation, the effect of the substrate mole ratio on UFA selectivity was greater than those of the others.en_US
dc.description.sponsorshipTurkish Scientific Research Council (TUBITAK) [107 O 110]en_US
dc.description.sponsorshipThis study was financially supported by the Turkish Scientific Research Council (TUBITAK) (Project Number. 107 O 110). Enzymes were generously provided by Novozym A/S (Denmark).en_US
dc.identifier.doi10.1007/s11746-010-1613-y
dc.identifier.endpage1307en_US
dc.identifier.issn0003-021X
dc.identifier.issue11en_US
dc.identifier.scopus2-s2.0-78149285185en_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.startpage1301en_US
dc.identifier.urihttps://doi.org/10.1007/s11746-010-1613-y
dc.identifier.urihttps://hdl.handle.net/11616/95171
dc.identifier.volume87en_US
dc.identifier.wosWOS:000283120500008en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofJournal of The American Oil Chemists Societyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectLipaseen_US
dc.subjectSelectivityen_US
dc.subjectAcidolysisen_US
dc.subjectUnsaturated fatty aciden_US
dc.subjectTripalmitinen_US
dc.subjectThermomyces lanuginosaen_US
dc.subjectRhizomucor mieheien_US
dc.subjectCandida antarcticaen_US
dc.titleC18 Unsaturated Fatty Acid Selectivity of Lipases During the Acidolysis Reaction Between Tripalmitin and Oleic, Linoleic, and Linolenic Acidsen_US
dc.typeArticleen_US

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