Surfactant-lactoperoxidase complex catalytically active in organic media

A surfactant-lactoperoxidase (LPO) complex catalytically active in organic solvents was developed by the emulsion coating method. The oxidation of 2,6 -dimethoxyphenol (2,6-DMP) was conducted by the surfactant-LPO complex in o rganic media. The LPO complex efficiently catalyzed the oxidation of 2,6-DM P in various organic solvents, although lyophilized LPO did not display the catalytic activity at all. To optimize the preparation and reaction condit ions for the surfactant-LPO complex, we examined the effects of pH value in the water pools of W/O emulsions, kinds of oxidants, and the nature of org anic solvents on the oxidation reaction. Its optimum activity was obtained when the pH value of the aqueous enzyme solution was adjusted to ca. 8 at t he preparation stage. The LPO complex exhibited the highest catalytic activ ity in chloroform when H2O2 was employed as the oxidant. Furthermore, the s torage stability of the surfactant-LPO complex was far better than that of the surfactant-horseradish peroxidase complex. This high storage stability of the LPO complex will be a benefit for industrial usage of peroxidases. ( C) 2000 Elsevier Science S.A. All rights reserved.