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

Research output: Contribution to journalArticle


Lipidic 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 -0.138V vs. Ag|AgCl at pH7.5, gave a catalytic current for lactose oxidation of 32.10μAcm-2 in MOPS buffer at pH7.5. The process carried out in the same solution but under direct electron conditions transfer resulted in a catalytic current of 9.22μAcm-2. Electrodes covered with CtCDH in a LCP film retained their catalytic activity after 28days showing a slightly increased current density after 6days.


  • Valentina Grippo
  • Su Ma
  • Roland Ludwig
  • Lo Gorton
  • Renata Bilewicz
External organisations
  • University of Natural Resources and Life Sciences, Vienna
  • University of Warsaw
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Chemical Sciences


  • Cellobiose dehydrogenase, Cubic phase, DET, MET
Original languageEnglish
Pages (from-to)134-141
Early online date2017 Oct 13
Publication statusPublished - 2019
Publication categoryResearch