Polymerization inhibitors are added to monomer solutions to prevent the inadvertent initiation of free radical polymerization during monomer storage and transportation. Residual levels of these inhibitors can be a source of irreproducibility in polymerization kinetics and can, therefore, disrupt efforts to control polymerization reactions for process optimization. We examined the feasibility of a non-capital-intensive separations approach for simply and efficiently removing the tert-butylcatechol storage inhibitor. The separations approach employs the enzyme tyrosinase to selectively oxidize the phenolic inhibitor, and the oxidation products are then strongly bound to a chitosan sorbent. For practicality we covalently immobilized the tyrosinase within chitosan gels to yield beads which served as both catalyst and sorbent for the phenolic inhibitor. These tyrosinase-containing chitosan gels were shown to be capable of removing low levels of tert-butylcatechol from both aqueous and organic phases and thus have the potential to be exploited for removing phenolic inhibitors in a range of polymerization operations. The use of tyrosinase-containing chitosan gels for waste minimization is discussed.