Improved Performance of Pseudomonas fluorescens lipase by covalent immobilization onto Amberzyme

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dc.authoridStavila, Erythrina/0000-0001-5167-3465
dc.authoridaslan, yakup/0000-0001-9668-9559
dc.authoridLoos, Katja/0000-0002-4613-1159
dc.authoridHandayani, Nurrahmi/0000-0002-0223-6039
dc.contributor.authorAslan, Yakup
dc.contributor.authorHandayani, Nurrahmi
dc.contributor.authorStavila, Erythrina
dc.contributor.authorLoos, Katja
dc.date.accessioned2024-12-24T19:32:55Z
dc.date.available2024-12-24T19:32:55Z
dc.date.issued2013
dc.departmentSiirt Üniversitesi
dc.description.abstractObjective: In this study, the conditions of covalent immobilization of Pseudomonas fluorescens lipase onto an oxirane-activated support (Amberzyme) were optimized to obtain a high activity yield. Furthermore, the operational and storage stabilities of immobilized lipase were tested. Methods: Optimum conditions for immobilization were determined by changing individually the conditions (pH from 5 to 9; buffer concentration from 0.025 to 2.5 M; amount of Amberzyme from 100 to 500 mg and duration of immobilization from 24 to 120 h). Amounts of protein and the activity of enzyme were determined by UV/Vis (PYE UNICAM SP8-200 UV/Vis spectrophotometer). Results: Immobilization conditions (pH and molar concentration of immobilization buffer, enzyme/support ratio and immobilization duration) significantly affected the immobilization efficiency. 100% immobilization yield and 145% activity yield were achieved by optimizing the immobilization conditions. Operational and storage stabilities of immobilized lipase were determined as well. The immobilized enzymes retained its activity for 20 consecutive batch reactions. Furthermore, the immobilized lipase showed a high storage stability as no decrease in its activity was observed for 20 days. Conclusion: Our results obtained in the present study are the best in the covalent immobilization of Pseudomonas fluorescens lipase in the literature. Therefore our future studies will focus on using the immobilized Pseudomonas fluorescens lipase for the production of biodiesel, hydrolysis of oils and various important esterification reactions.
dc.description.sponsorshipCouncil of Higher Education of Turkey
dc.description.sponsorshipThe authors acknowledge Rohm and Haas Company for their generous gift by providing Amberzyme. Y.A. also acknowledge The Council of Higher Education of Turkey for their financial support.
dc.identifier.doi10.5505/tjb.2013.30085
dc.identifier.endpage318
dc.identifier.issn0250-4685
dc.identifier.issn1303-829X
dc.identifier.issue3
dc.identifier.startpage313
dc.identifier.urihttps://doi.org/10.5505/tjb.2013.30085
dc.identifier.urihttps://hdl.handle.net/20.500.12604/7885
dc.identifier.volume38
dc.identifier.wosWOS:000328162700011
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.language.isoen
dc.publisherTurkish Biochem Soc
dc.relation.ispartofTurkish Journal of Biochemistry-Turk Biyokimya Dergisi
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_20241222
dc.subjectamberzyme
dc.subjectcovalent attachment
dc.subjectenzyme immobilization
dc.subjectlipase
dc.subjectPseudomonas fluorescens
dc.titleImproved Performance of Pseudomonas fluorescens lipase by covalent immobilization onto Amberzyme
dc.typeArticle

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