Journal article
Hydrogel-Immobilized Supercharged Proteins
EC Campbell, J Grant, Y Wang, M Sandhu, RJ Williams, DR Nisbet, AW Perriman, DW Lupton, CJ Jackson
Advanced Biosystems | Published : 2018
Abstract
The remarkable catalytic potential of enzymes in chemical synthesis, environmental bioremediation, and medical therapeutics is limited by their longevity and stability. Immobilization of enzymes on solid supports is demonstrated to improve the stability of biocatalysts but often relies on multiple chemical steps for covalent attachment and is limited by the physical properties of the various supports. Here, production of enzyme: hydrogel complexes is described via engineering of a cationic supercharged phosphotriesterase. These enzyme: hydrogel complexes are remarkably robust displaying no loss of catalytic activity after 80 d of use and up to 105 turnovers when used in a flow reactor at cat..
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Awarded by Engineering and Physical Sciences Research Council
Funding Acknowledgements
A.W.P. would like to acknowledge the Engineering and Physical Research Council (EPSRC) for support (Early Career Fellowship EP/K026720/1). C.J.J. and D.W.L. would like to acknowledge the Australian Research Council (ARC) for support (Discovery Projects (DP) and FT programs). E.C. would like to thank the Australian Government for support through the Australian Postgraduate Award (APA), and the Australian National University (ANU) for funding through the Alan Sargeson and Research School of Chemistry Scholarships. E.C. performed experiments and analyzed results and wrote the paper. J.G., Y.W., and M.S. performed experiments and analyzed results. R.J.W. and D.R.N. designed experiments and analyzed results. A.W.P. conceived the project and analyzed results. D.W.L. designed experiments and analyzed results. C.J.J. conceived the project, designed experiments, analyzed results, and wrote the paper with input from all authors.