Polymer-Based Protein Engineering Enables Molecular Dissolution of Chymotrypsin in Acetonitrile
| Autor: | Hironobu Murata, Chad Cummings, Krzysztof Matyjaszewski, Alan J. Russell |
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| Rok vydání: | 2016 |
| Předmět: |
Aqueous solution
Polymers and Plastics Chemistry Atom-transfer radical-polymerization Organic Chemistry Substrate (chemistry) 02 engineering and technology Transesterification 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences 0104 chemical sciences Inorganic Chemistry Propanol chemistry.chemical_compound Materials Chemistry Anhydrous Organic chemistry Solubility 0210 nano-technology Acetonitrile |
| Zdroj: | ACS Macro Letters. 5:493-497 |
| ISSN: | 2161-1653 |
| DOI: | 10.1021/acsmacrolett.6b00137 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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