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- W2331750246 abstract "While most effective in aqueous environments, enzymes are also able to catalyze reactions in essentially anhydrous organic media. Enzyme activity in organic solvents is limited as a result of inefficient substrate binding, lack of solubility, and inactivation by hydrophilic anhydrous solvents. With these facts in mind, atom transfer radical polymerization was used to synthesize chymotrypsin-poly(2-(dimethylamino)ethyl methacrylate) (CT-pDMAEMA) conjugates designed to be soluble and active in acetonitrile. CT-pDMAEMA solubility in organic solvents and the rate of CT-pDMAEMA-catalyzed transesterification in acetonitrile were examined at a range of water (0-15 M) and propanol (0.01-5 M) concentrations. The conjugates were soluble at the molecular scale in several organic solvents, exhibited good substrate binding with N-acetyl l-phenylalanine thiophenylester (KM as low as 17 mM), and had an activity (peak activity 330 μM/min/mg enzyme) many orders of magnitude higher than that of the insoluble native enzyme." @default.
- W2331750246 created "2016-06-24" @default.
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- W2331750246 date "2016-03-30" @default.
- W2331750246 modified "2023-09-23" @default.
- W2331750246 title "Polymer-Based Protein Engineering Enables Molecular Dissolution of Chymotrypsin in Acetonitrile" @default.
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- W2331750246 doi "https://doi.org/10.1021/acsmacrolett.6b00137" @default.
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