An enzyme-mimic polymer was prepared by the surface molecular imprinting technique. In the active site of the polymer, a substrate analog was imprinted through the complex formation between a cobalt ion and alkyl imidazole that functions as the hydrolysis catalysis. The enzymatic performance of the imprinted polymer was evaluated by the hydrolysis reaction of an amino acid ester. Based on the Michaelis-Menten analysis, Vmax and Km were obtained. The imprinted polymer shows a high activity compared to that of the control unimprinted polymer. The result was supported by a low Km value of the imprinted polymer, indicating a high affinity to the target substrate. The enzyme-mimic polymer was found to possess a substrate specificity by using several substrates that have a different structure. A computational modeling also supports the structure of the imprinted sites formed on the polymer surface.
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