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Hydrogel-immobilized supercharged proteins

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Version 2 2024-06-03, 15:41
Version 1 2019-05-15, 09:44
journal contribution
posted on 2024-06-03, 15:41 authored by EC Campbell, J Grant, Y Wang, M Sandhu, Richard WilliamsRichard Williams, DR Nisbet, AW Perriman, DW Lupton, CL Jackson
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 10 5 turnovers when used in a flow reactor at catalyst loadings as low as 0.0008 mol%. In addition, exceptional resilience to organic solvents is observed. The use of enzyme: hydrogel complexes is likely to be of value in a diverse range of applications such as enantioselective continuous-flow chemistry, detoxification of poisons, and the formation of functionalized biomaterials.

History

Journal

Advanced biosystems

Volume

2

Pagination

1-11

Location

Chichester, Eng.

Open access

  • Yes

eISSN

2366-7478

Language

eng

Publication classification

C Journal article, C1 Refereed article in a scholarly journal

Copyright notice

2018, WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim

Issue

7

Publisher

John Wiley & Sons