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Graphene-oxide-based enzyme nanoarchitectonics for substrate channeling

Mathesh Shanmugam, Motilal, Liu, Jingquan, Barrow, Colin J and Yang, Wenrong 2017, Graphene-oxide-based enzyme nanoarchitectonics for substrate channeling, Chemistry - a European journal, vol. 23, no. 2, pp. 304-311, doi: 10.1002/chem.201604348.

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Title Graphene-oxide-based enzyme nanoarchitectonics for substrate channeling
Author(s) Mathesh Shanmugam, Motilal
Liu, Jingquan
Barrow, Colin JORCID iD for Barrow, Colin J orcid.org/0000-0002-2153-7267
Yang, WenrongORCID iD for Yang, Wenrong orcid.org/0000-0001-8815-1951
Journal name Chemistry - a European journal
Volume number 23
Issue number 2
Start page 304
End page 311
Total pages 8
Publisher Wiley-Blackwell
Place of publication London, Eng.
Publication date 2017-01-05
ISSN 0947-6539
1521-3765
Keyword(s) enzyme immobilization
enzyme nanoarchitectonics
enzymes
graphene
substrate channeling
Science & Technology
Physical Sciences
Chemistry, Multidisciplinary
Chemistry
Glucose-oxidase
Horseradish-peroxidase
Molecular films
Angstrom resolution
Sequential reaction
Modified-electrode
DNA scaffolds
Cytochrome-C
Protein
Immobilization
Summary The controlled spatial organization or compartmentalization of multi-enzyme cascade reactions to transfer a substrate from one enzyme to another for substrate channeling on scaffolds has sparked increasing interest in recent years. Here, we use graphene oxides to study the dependence of the activity of cascade reactions in a closely packed, randomly immobilized enzyme system on a 2 D scaffold. We first observe that the hydrophobicity of graphene oxides and various enzyme architectures for co-immobilized systems are important attributes for achieving high product-conversion rates. A transient time close to 0 s can be achieved if enzymes are randomly immobilized close to one another, owing to direct molecular channeling. This contributes to overcoming complications regarding control of the spatial arrangement of the enzymes. Furthermore, a fabricated bienzyme paper can be used for glucose detection with high stability, reusability, and enhanced substrate channeling. Our findings provide new guidance for enzyme orientation on 2 D scaffolds, which may be extrapolated to other multienzyme cascade systems.
Language eng
DOI 10.1002/chem.201604348
Field of Research 030302 Nanochemistry and Supramolecular Chemistry
03 Chemical Sciences
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2017, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
Persistent URL http://hdl.handle.net/10536/DRO/DU:30090331

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Created: Mon, 03 Apr 2017, 12:59:34 EST

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