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Opening lids: modulation of lipase immobilization by graphene oxides

Mathesh, Motilal, Luan, Binquan, Akanbi, Taiwo, Weber, Jeffrey K, Liu, Jingquan, Barrow, Colin, Zhou, Ruhong and Yang, Wenrong 2016, Opening lids: modulation of lipase immobilization by graphene oxides, ACS catalysis, vol. 6, no. 7, pp. 4760-4768, doi: 10.1021/acscatal.6b00942.

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Title Opening lids: modulation of lipase immobilization by graphene oxides
Author(s) Mathesh, Motilal
Luan, Binquan
Akanbi, TaiwoORCID iD for Akanbi, Taiwo orcid.org/0000-0002-9249-6503
Weber, Jeffrey K
Liu, Jingquan
Barrow, ColinORCID iD for Barrow, Colin orcid.org/0000-0002-2153-7267
Zhou, Ruhong
Yang, WenrongORCID iD for Yang, Wenrong orcid.org/0000-0001-8815-1951
Journal name ACS catalysis
Volume number 6
Issue number 7
Start page 4760
End page 4768
Total pages 9
Publisher American Chemical Society
Place of publication Washington D.C., Wash.
Publication date 2016-07-01
ISSN 2155-5435
Keyword(s) graphene oxides
lipase
hydrophobic
enzyme papers
simulation
Summary Lipases, which can be immobilized and reused for many reaction cycles, are important enzymes with many industrial applications. A key challenge in lipase immobilization for catalysis is to open the lipase lid and maintain it in an open conformation in order to expose its active site. Here we have designed "tailor-made" graphene-based nanosupports for effective lipase (QLM) immobilization through molecular engineering, which is in general a grand challenge to control biophysicochemical interactions at the nano-bio interface. It was observed that increasing hydrophobic surface increased lipase activity due to opening of the helical lid present on lipase. The molecular mechanism of lid opening revealed in molecular dynamics simulations highlights the role of hydrophobic interactions at the interface. We demonstrated that the open and active form of lipase can be achieved and tuned with an optimized activity through chemical reduction of graphene oxide. This research is a major step toward designing nanomaterials as a platform for enhancing enzyme immobilization/activity.
Language eng
DOI 10.1021/acscatal.6b00942
Field of Research 030302 Nanochemistry and Supramolecular Chemistry
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 ©2016, American Chemical Society
Persistent URL http://hdl.handle.net/10536/DRO/DU:30085387

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Created: Tue, 15 Nov 2016, 13:13:51 EST

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