williams-hydrogelimmobilized-2018.pdf (2.18 MB)
Hydrogel-immobilized supercharged proteins
journal contribution
posted on 2018-07-01, 00:00 authored by E C Campbell, J Grant, Y Wang, M Sandhu, Richard WilliamsRichard Williams, D R Nisbet, A W Perriman, D W Lupton, C L JacksonThe 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 biosystemsVolume
2Issue
7Pagination
1 - 11Publisher
John Wiley & SonsLocation
Chichester, Eng.Publisher DOI
Link to full text
eISSN
2366-7478Language
engPublication classification
C Journal article; C1 Refereed article in a scholarly journalCopyright notice
2018, WILEY‐VCH Verlag GmbH & Co. KGaA, WeinheimUsage metrics
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