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dc.contributor.authorAlbuquerque, Tiago L.deen_US
dc.contributor.authorRueda, Nazzolyen_US
dc.contributor.authordos Santos, Jose C.S.en_US
dc.contributor.authorBarbosa, Oveimaren_US
dc.contributor.authorOrtiz, Claudiaen_US
dc.contributor.authorBinay, Barışen_US
dc.contributor.authorÖzdemir, Eceen_US
dc.contributor.authorGonçalves, Luciana R.B.en_US
dc.contributor.authorFernandez-Lafuente, Robertoen_US
dc.date.accessioned2017-07-10T11:14:56Z
dc.date.available2017-07-10T11:14:56Z
dc.date.issued2016
dc.identifier.citationAlbuquerque, T., Rueda, N., dos Santos, J., Barbosa, O., Ortiz, C., Binay, B., Özdemir, E., Gonçalves, L., Fernandez-Lafuente, R. (2016). Easy stabilization of interfacially activated lipases using heterofunctional divinyl sulfone activated-octyl agarose beads. Modulation of the immobilized enzymes by altering their nanoenvironment. Process Biochemistry. 51.7, 865-874.en_US
dc.identifier.issn1359-5113
dc.identifier.urihttps://hdl.handle.net/20.500.12294/844
dc.identifier.urihttps://doi.org/10.1016/j.procbio.2016.04.002
dc.descriptionBinay, Barış (Arel Author)en_US
dc.description.abstractOctyl-agarose is a support that permits the one step immobilization, stabilization and purification of lipases. However, the enzyme may be released from the support under drastic conditions. This paper describes a new heterofunctional support, octyl agarose beads activated with divinyl sulfone, that has proved to be useful to produce very stable and active biocatalysts of lipases from Candida rugosa (CRL), Rhizomucor miehei (RML) and Thermomyces lanuginosus (TLL), able to work under any reaction conditions without risking enzyme desorption. The three enzymes failed inimmobilizationonglyoxyl-octyl supports for different reasons. The immobilization at pH 5 permitted to keep the good properties of octyl agarose. Further incubation at pH 8 permitted to establish at least one covalent enzyme-support bond per enzyme molecule (preventing the risk of enzyme desorption), avoiding the inactivation produced at pH 10, and the final result is that all three new biocatalysts are more active than the octyl-glyoxyl counterparts and much more stable (e.g., 20 using CRL). The end of the enzyme-support reaction was achieved via blocking the vinylsulfone groups with different nucleophiles (cationic, anionic, hydrophobic, etc). This not only determined the final enzyme stability, but also the activity, selectivity and even specificity ofthe different immobilized preparations.en_US
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectLipase Interfacial Activationen_US
dc.subjectHeterofunctional Supporten_US
dc.subjectDivinyl Sulfoneen_US
dc.subjectEnzyme Hyperactivationen_US
dc.subjectEnzyme Stabilizationen_US
dc.subjectCovalent Immobilizationen_US
dc.titleEasy stabilization of interfacially activated lipases using heterofunctional divinyl sulfone activated-octyl agarose beads. Modulation of the immobilized enzymes by altering their nanoenvironmenten_US
dc.typearticleen_US
dc.relation.journalProcess Biochemistryen_US
dc.contributor.departmentİstanbul Arel Üniversitesi, Fen-Edebiyat Fakültesi, Moleküler Biyoloji ve Genetik Bölümüen_US
dc.contributor.authorIDTR16264en_US
dc.identifier.volume51en_US
dc.identifier.issue7en_US
dc.identifier.startpage865en_US
dc.identifier.endpage874en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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