Immobilization of horseradish peroxidase by electrospun fibrous membranes for adsorption and degradation of pentachlorophenol in water.

Horseradish peroxidase (HRP) is successfully in situ encapsulated into the poly(D,L-lactide-co-glycolide) (PLGA)/PEO-PPO-PEO (F108) electrospun fibrous membranes (EFMs) by emulsion electrospinning. The adsorption and degradation of pentachlorophenol (PCP) by HRP-EFMs are investigated. The experimental results show that the sorption kinetic of PCP on EFMs follows the pseudo-second-order model, and the sorption capacity is as high as 44.69 mg g(-1). The sorption mechanisms of EFMs for PCP can be explained by hydrogen bonding interactions, hydrophobic interactions and π-π bonding interactions. Profiting from the strong adsorption, the removal of PCP can be dramatically enhanced by the interaction of adsorbed PCP and HRP on the surface of EFMs. For PCP degradation, the optimal pH values for free HRP and immobilized HRP are 4 and 2-4, respectively. As pH>4.7, no adsorption and degradation are observed due to the deprotonation of PCP. The removal percentages reach 83% and 47% for immobilized HRP and free HRP, respectively, at 25 ± 1°C. The presence of humic acid can inhibit the activity of HRP and decreases the adsorption capacity of PCP because of competitive adsorption. The operational and storage stability of immobilized HRP are highly improved through emulsion electrospinning.