Comparison of the performance of entrapped and covalently immobilized lipase in the synthesis of pear flavor

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dc.contributor.authorOzyilmaz, Gul
dc.contributor.authorYagiz, Esra
dc.date.accessioned2024-09-18T20:29:35Z
dc.date.available2024-09-18T20:29:35Z
dc.date.issued2017
dc.departmentHatay Mustafa Kemal Üniversitesien_US
dc.description.abstractIntroduction: Although aroma esters are produced mostly by a chemical method that requires the use of aggressive chemical catalysts, enzymatic esterification has been very favored during previous two decades. The main aim of this study was to investigate the commercially important pear flavor, hexyl acetate (HAc), by the catalysis of immobilized lipase samples and to optimize the immobilization and operational conditions in detail. Methods: Lipases from Candida rugosa (CRL) and porcine pancreas (PPL) were immobilized using biodegradable polysaccharides, by entrapment in calcium alginate/chitosan composite gel (CRLCa-Alg/Chi and PPLCa-Alg/Chi) and by covalent binding onto the chitosan (CRLChi and PPLChi) carrier. Results: Among the several organic media, the highest esterification activites were observed in heptane. HAc yield decreased when substrate concentrations were higher than 50 or 75 mM. Yield increased with increase in reaction time up to the 5th hour in the batch type reactor while it increased during the 8 h reaction time for fixed bed reactors with lower yields. Discussion and conclusions: As well as synthesis conditions, immobilization parameters also affected HAc productivity. The amount of water in the microenvironment of lipase is so important not only for gaining its active conformation but only for the reaction direction.en_US
dc.description.sponsorshipScientific Research Units of the Mustafa Kemal University [09M 0501]en_US
dc.description.sponsorshipThe authors gratefully acknowledge the financial support for this work by the Scientific Research Units of the Mustafa Kemal University (Project No.: 09M 0501).en_US
dc.identifier.doi10.1515/tjb-2016-0110
dc.identifier.endpage347en_US
dc.identifier.issn0250-4685
dc.identifier.issn1303-829X
dc.identifier.issue3en_US
dc.identifier.scopus2-s2.0-85021756126en_US
dc.identifier.scopusqualityQ3en_US
dc.identifier.startpage339en_US
dc.identifier.urihttps://doi.org/10.1515/tjb-2016-0110
dc.identifier.urihttps://hdl.handle.net/20.500.12483/10952
dc.identifier.volume42en_US
dc.identifier.wosWOS:000405121500012en_US
dc.identifier.wosqualityQ4en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherWalter De Gruyter Gmbhen_US
dc.relation.ispartofTurkish Journal of Biochemistry-Turk Biyokimya Dergisien_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectLipaseen_US
dc.subjectHexyl acetateen_US
dc.subjectPear flavoren_US
dc.subjectAlginateen_US
dc.subjectChitosanen_US
dc.subjectImmobilizationen_US
dc.subjectResponse surface methodologyen_US
dc.titleComparison of the performance of entrapped and covalently immobilized lipase in the synthesis of pear flavoren_US
dc.typeArticleen_US

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