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Phenol Removal by Immobilized Horseradish Peroxidase

Horseradish peroxidase was successfully encapsulated in calcium alginate for phenol removal. The optimum gelation condition was found to be 0.75%w/v of sodium alginate solution and 4.5% w/v of calcium chloride hexahydrate. Upon immobilization, the pH profile of enzyme activity changed as it showed a higher relative value in basic and acidic solutions. It was also observed that enzyme activity retention of encapsulated HRP was independent of enzyme concentration. Besides, for each phenol concentration, there would be an enzyme concentration beyond which it had no significant effect on phenol removal. Investigation of phenol removal with time for both encapsulated and free enzymes showed that the encapsulated enzyme had a lower efficiency compared to the same concentration of the free enzyme; however, the capsules were reusable up to four cycles without any changes in their retention activity. The optimum ratio of hydrogen peroxide/phenol was found to depend on phenol concentration and that it varied from 0.94 to 1.15 for phenol concentrations between 2-10 raM.