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Cellobiose dehydrogenase hosted in lipidic cubic phase to improve catalytic activity and stability.

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cris.lastimport.scopus2024-02-12T20:27:23Z
dc.abstract.enLipidic cubic phase systems (LCPs) are excellent carriers for immobilized enzymes due to their biocompatibility and well-defined nanoporous structure. Lipidic cubic phases act as a convenient matrix to incorporate enzymes and hold them in the vicinity of electrode surfaces in their fully active forms. Corynascus thermophilus cellobiose dehydrogenase (CtCDH) was trapped in a monoolein cubic phase, which increased not only its stability, but also its catalytic performance with both enhanced mediated and direct electron transfer with electrodes. For studies of mediated electron transfer, three mediators with different formal potentials (E°′) were employed: horse-heart cytochrome c (cyt c), electron acceptor active with the cytochrome domain of CtCDH, and 2,6-dichlorophenolindophenol (DCPIP) as well as hexaammineruthenium(II) chloride [Ru(NH3)Cl2] both electron acceptors with the dehydrogenase domain. Ru(NH3)Cl2, having the most negative E°′ of − 0.138 V vs. Ag | AgCl at pH 7.5, gave a catalytic current for lactose oxidation of 32.10 μA cm− 2 in MOPS buffer at pH 7.5. The process carried out in the same solution but under direct electron conditions transfer resulted in a catalytic current of 9.22 μA cm− 2. Electrodes covered with CtCDH in a LCP film retained their catalytic activity after 28 days showing a slightly increased current density after 6 days.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorBilewicz, Renata
dc.contributor.authorGorton, Lo
dc.contributor.authorGrippo, Valentina
dc.contributor.authorMa, Su
dc.contributor.authorLudwig, Roland
dc.date.accessioned2024-01-24T19:04:55Z
dc.date.available2024-01-24T19:04:55Z
dc.date.issued2019
dc.description.financeNie dotyczy
dc.description.volume125
dc.identifier.doi10.1016/J.BIOELECHEM.2017.10.003
dc.identifier.issn1567-5394
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/102789
dc.languageeng
dc.pbn.affiliationchemical sciences
dc.relation.ispartofBioelectrochemistry
dc.relation.pages134-141
dc.rightsClosedAccess
dc.sciencecloudnosend
dc.subject.enCellobiose dehydrogenase
dc.subject.enCubic phase
dc.subject.enDET
dc.subject.enMET
dc.titleCellobiose dehydrogenase hosted in lipidic cubic phase to improve catalytic activity and stability.
dc.typeJournalArticle
dspace.entity.typePublication