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Solubilizing and stabilizing proteins in anhydrous lonic liquids through formation of protein-polymer surfactant nanoconstructs

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Title: Solubilizing and stabilizing proteins in anhydrous lonic liquids through formation of protein-polymer surfactant nanoconstructs
Authors: Brogan, AP
Hallett, JP
Item Type: Journal Article
Publication Date: 2017-03-14T07:00:12Z
Abstract: Nonaqueous biocatalysis is rapidly becoming a desirable tool for chemical and fuel synthesis in both the laboratory and industry. Similarly, ionic liquids are increasingly popular anhydrous reaction media for a number of industrial processes. Consequently, the use of enzymes in ionic liquids as efficient, environment-friendly, commercial biocatalysts is highly attractive. However, issues surrounding the poor solubility and low stability of enzymes in truly anhydrous media remain a significant challenge. Here, we demonstrate for the first time that engineering the surface of a protein to yield protein-polymer surfactant nanoconstructs allows for dissolution of dry protein into dry ionic liquids. Using myoglobin as a model protein, we show that this method can deliver protein molecules with near native structure into both hydrophilic and hydrophobic anhydrous ionic liquids. Remarkably, using temperature-dependent synchrotron radiation circular dichroism spectroscopy to measure half-denaturation temperatures, our results show that protein stability increases by 55 °C in the ionic liquid as compared to aqueous solution, pushing the solution thermal denaturation beyond the boiling point of water. Therefore, the work presented herein could provide a platform for the realization of biocatalysis at high temperatures or in anhydrous solvent systems.
Issue Date: 14-Mar-2016
Date of Acceptance: 1-Mar-2016
URI: http://hdl.handle.net/10044/1/31073
DOI: http://dx.doi.org/10.1021/jacs.5b13425
ISSN: 1520-5126
Publisher: American Chemical Society
Start Page: 4494
End Page: 4501
Journal / Book Title: Journal of the American Chemical Society
Volume: 138
Issue: 13
Copyright Statement: © 2016 American Chemical Society. This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Chemical Theory and Computation after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/jacs.5b13425
Sponsor/Funder: Engineering & Physical Science Research Council (EPSRC)
Funder's Grant Number: EP/K038648/1
Keywords: General Chemistry
Chemical Sciences
Publication Status: Published
Appears in Collections:Faculty of Engineering
Chemistry
Chemical Engineering
Faculty of Natural Sciences



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