4.7 Article

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

期刊

BIOELECTROCHEMISTRY
卷 125, 期 -, 页码 134-141

出版社

ELSEVIER SCIENCE SA
DOI: 10.1016/j.bioelechem.2017.10.003

关键词

Cellobiose dehydrogenase; Cubic phase; DET; MET

资金

  1. FP7-People-2013-ITN Grant 'Bioenergy, Biofuel Cells: From fundamentals to application of bioelectrochemistry' [607793]

向作者/读者索取更多资源

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 degrees') 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)Cl-2] both electron acceptors with the dehydrogenase domain. Ru(NH3)Cl-2, having the most negative E degrees' of -0.138 V vs. Ag vertical bar AgCl at pH 7.5, gave a catalytic current for lactose oxidation of 32.10 mu A 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 mu A 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. (C) 2017 Elsevier B.V. All rights reserved.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据