Cross-Linked Enzyme Aggregates of Chloroperoxidase: Synthesis, Optimization and Characterization

In this study we have optimized the conditions to precipitate and cross-link the enzyme chloroperoxidase (EC 1.11.1.10) from Caldariomyces fumago (CPO) using 1,2-dimethoxyethane as the precipitating agent. The coprecipitation of the enzyme with albumin and pentaethylenehexamine was needed for optimum results, presumably due to the low number of lysines available in CPO. The enzyme was immobilized with an activity recovery of 68%. The cross-linked enzyme aggregate showed higher temperature and pH stability, and better hydrogen peroxide tolerance than the free enzyme.