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2,4-dichlorophenol enzymatic removal and its kinetic study using HRP crosslinked to nano spray dried poly(lactic-co-glycolic acid) fine particles.

Research paper by Laura Amina LA Dahili, Endre E Nagy, Tivadar T Feczkó

Indexed on: 09 Feb '17Published on: 09 Feb '17Published in: Journal of microbiology and biotechnology



Abstract

Horseradish peroxidase (HRP) catalyzes the oxidation of aromatic compounds by hydrogen peroxide via insoluble polymer formation, which can be precipitated from the wastewater. For HRP immobilization poly(lactic-co-glycolic acid) (PLGA) fine carrier supports were produced by Nano Spray Dryer B-90. Immobilized HRP was used to remove the persistent 2,4-dichlorophenol from model wastewater. Both extracted (9-16 U/g) and purified HRP (11-25 U/g) retained their activity to a high extent after crosslinking to the PLGA particles. The immobilized enzyme activity was substantially higher in both of the acidic and the alkaline pH region compared to the free enzyme. Optimally 98 % of the 2,4-dichlorophenol could be eliminated using immobilized HRP due to catalytic removal and partly to adsorption on the carrier supports. Immobilized enzyme kinetics for 2,4-dichlorophenol elimination was studied for the first time, and it could be concluded that competitive product inhibition took place.