@article{Brogan:2016:10.1021/jacs.5b13425,
author = {Brogan, AP and Hallett, JP},
doi = {10.1021/jacs.5b13425},
journal = {Journal of the American Chemical Society},
pages = {4494--4501},
title = {Solubilizing and stabilizing proteins in anhydrous lonic liquids through formation of protein-polymer surfactant nanoconstructs},
url = {http://dx.doi.org/10.1021/jacs.5b13425},
volume = {138},
year = {2016}
}

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TY  - JOUR
AB  - 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.
AU  - Brogan,AP
AU  - Hallett,JP
DO  - 10.1021/jacs.5b13425
EP  - 4501
PY  - 2016///
SN  - 1520-5126
SP  - 4494
TI  - Solubilizing and stabilizing proteins in anhydrous lonic liquids through formation of protein-polymer surfactant nanoconstructs
T2  - Journal of the American Chemical Society
UR  - http://dx.doi.org/10.1021/jacs.5b13425
UR  - http://www.ncbi.nlm.nih.gov/pubmed/26976718
UR  - http://hdl.handle.net/10044/1/31073
VL  - 138
ER  - 

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