Hemo-acrylic polymers as catalyst for the oxidative dehalogenation of 2,4,6-trichlorophenol. Chloroperoxidase's mimic imprinting effects

Acrylic polymers with catalytic activity for the oxidative degradation of 2,4,6-trichlorophenol (TCP) were developed. In order to mimic the active site of chloroperoxidase (CPO), chloro-iron(III)-protoporphyrin IX was used as the catalytic centre, and methacrylamide (MA) and 4-vinylpyridine (VPY) were used as the monomers that build up the active sites. Taking as basis 3:1 (w/w) acid:basic aminoacidic composition of CPO, three MA:VPY combinations were tested: one keeping the same ratio (3:1) i.e. 25% VPY in the functional monomer mixture, one with lower content of the basic monomer (9:1) i.e. 10% VPY, and one with higher concentration of it (1:1) i.e. 50% VPY. Polymers synthesized with the lowest VPY content exhibited the highest catalytic efficiency, which was improved by the creation of specific TCP binding sites through molecular imprinting technology. In these way, synthetic enzymes with useful properties for analytical and bioremediation applications were obtained.

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► We synthesize hemo-acrylic polymers that mimic chloroperoxidase.
► Catalysts for the oxidative dehalogenation of 2,4,6-trichlorophenol.
► We use a combination of methacrylamide and 4-vinylpyridine as functional monomers.
► The polymer with 9:1 MA:VPY exhibited the highest catalytic efficiency.
► Substrate selectivity was introduced by the use of molecular imprinting technology.