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Received August 12, 2013
Accepted December 13, 2013
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Enzyme attached on polymeric micelles as a nanoscale reactor
Department of Chemical and Biomedical Engineering, Cleveland State University, 1960 East 24th Street, Cleveland, Ohio 44115-2214, USA 1Department of International Development Engineering, Tokyo Institute of Technology, 2-12-1 Ookayama, Meguro-ku, Tokyo 152-8550, Japan
m.lee68@csuohio.edu
Korean Journal of Chemical Engineering, February 2014, 31(2), 188-193(6), 10.1007/s11814-013-0277-3
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Abstract
Similar to what lipase does, a surface-active enzyme was developed by attaching peroxidase on combshaped polymaleic anhydride-alt-1-tetradecene (PMA-TD) in a microemulsion system composed of n-butyl acetate and buffer solution, and its catalytic characteristics of polyphenol synthesis were investigated in an aqueous solution. The modified peroxidase with PMA-TD tended to form self-assembled aggregates like micelles in the aqueous solution and could be concentrated at solvent/water interfaces without unfolding of the enzyme. The efficiency of conversion of 2,4-dichlorophenol to phenolic oligomers was approximately 2-fold improved with the modified peroxidase compared to native peroxidase. The Km and Vmax values for the modified peroxidase were 1.5-fold lower and 2-fold higher, respectively. The hydrodynamic diameter of the micelle on the modified peroxidase increased with the reaction time, indicating that phenolic products were accumulated in the hydrophobic interior of micelles. In addition, the molecular weight (MW) of phenolic polymers was much larger in the system with the modified peroxidase. These observations implied that the modified peroxidase with hydrophobic side chains formed micellar structures by solubilization of phenolic products and further polymerization reaction could occur in the hydrophobic interior of the micelles.
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