The Electrosome: A Surface-Displayed Enzymatic Cascade in a Biofuel Cell's Anode and a High-Density Surface-Displayed Biocathodic Enzyme.

Autor:	Szczupak A; Department of Life Sciences and the Ilse Katz Institute for Nanoscale Science and Technology, P.O. Box 653, 8410501 Beer-Sheva, Israel. alonszcz@post.bgu.ac.il., Aizik D; Department of Life Sciences and the Ilse Katz Institute for Nanoscale Science and Technology, P.O. Box 653, 8410501 Beer-Sheva, Israel. dror12321@gmail.com., Moraïs S; Department of Biomolecular Sciences, Weizmann Institute of Science, 234 Herzl St., P.O. Box 26, 7610001 Rehovot, Israel. sarahv@weizmann.ac.il., Vazana Y; Department of Biomolecular Sciences, Weizmann Institute of Science, 234 Herzl St., P.O. Box 26, 7610001 Rehovot, Israel. yael.vazana@sial.com., Barak Y; Department of Chemical Research Support, Weizmann Institute of Science, 234 Herzl St., P.O. Box 26, 7610001 Rehovot, Israel. yoav.barak@weizmann.ac.il., Bayer EA; Department of Biomolecular Sciences, Weizmann Institute of Science, 234 Herzl St., P.O. Box 26, 7610001 Rehovot, Israel. ed.bayer@weizmann.ac.il., Alfonta L; Department of Life Sciences and the Ilse Katz Institute for Nanoscale Science and Technology, P.O. Box 653, 8410501 Beer-Sheva, Israel. alfontal@bgu.ac.il.
Jazyk:	angličtina
Zdroj:	Nanomaterials (Basel, Switzerland) [Nanomaterials (Basel)] 2017 Jun 23; Vol. 7 (7). Date of Electronic Publication: 2017 Jun 23.
DOI:	10.3390/nano7070153
Abstrakt:	The limitation of surface-display systems in biofuel cells to a single redox enzyme is a major drawback of hybrid biofuel cells, resulting in a low copy-number of enzymes per yeast cell and a limitation in displaying enzymatic cascades. Here we present the electrosome, a novel surface-display system based on the specific interaction between the cellulosomal scaffoldin protein and a cascade of redox enzymes that allows multiple electron-release by fuel oxidation. The electrosome is composed of two compartments: (i) a hybrid anode, which consists of dockerin-containing enzymes attached specifically to cohesin sites in the scaffoldin to assemble an ethanol oxidation cascade, and (ii) a hybrid cathode, which consists of a dockerin-containing oxygen-reducing enzyme attached in multiple copies to the cohesin-bearing scaffoldin. Each of the two compartments was designed, displayed, and tested separately. The new hybrid cell compartments displayed enhanced performance over traditional biofuel cells; in the anode, the cascade of ethanol oxidation demonstrated higher performance than a cell with just a single enzyme. In the cathode, a higher copy number per yeast cell of the oxygen-reducing enzyme copper oxidase has reduced the effect of competitive inhibition resulting from yeast oxygen consumption. This work paves the way for the assembly of more complex cascades using different enzymes and larger scaffoldins to further improve the performance of hybrid cells. Competing Interests: The authors declare no conflict of interest.
Databáze:	MEDLINE
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