Wee1B Is an Oocyte-Specific Kinase Involved in the Control of Meiotic Arrest in the Mouse

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Enzyme Attached on Polymeric Micelles as a Nanoscale Reactor

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 K m and V max 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

Enzyme Attached on Polymeric Micelles as a Nanoscale Reactor

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 K m and V max 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