从图中能够看出，随着酪氨酸酶浓度不断增加，polyoxometalat

It can be seen from the figure that as the concentration of tyrosinase increases, the cyclic voltammogram response current of polyoxometalates catalyzing tyrosinase gradually weakens, but the magnitude of the weakening is small, indicating that polyoxometalates catalyzes tyrosinase. Has a certain effect. This may be because tyrosinase is a neutral molecule, so it is not hindered by static electricity from the outermost anion P2Mo18 and can enter the membrane. The use of polypyrrole to separate P2Mo18O626-the resulting multilayer membrane can help to obtain greater catalysis The current makes the electrode surface have catalytic ability.

As can be seen from the figure, as the concentration of tyrosinease increases, the circulating voanto response current of polyoxometalates catalytic tyrosinease gradually decreases, but decreases by a smaller margin, indicating that polyoxometalates play a role in catalysis of tyrosinease. This may be because tyrosine enzyme is a neutral molecule, so it is not hindered by the electrostatic obstruction of the outermost anion P2Mo18 and can enter the membrane, the use of polycyclic chrysanthemum interval P2Mo18O626 - the resulting multi-layer membrane can help to obtain a larger catalytic current, so that the electrode surface has catalytic capacity.

It can be seen from the figure that with the increase of tyrosinase concentration, the cyclic voltammetric response current of tyrosinase catalyzed by polyoxometalates gradually decreases, but the weakening amplitude is small, which indicates that polyxmetalates play a certain role in the catalysis of tyrosinase. This may be due to the fact that tyrosinase is a neutral molecule, so it can enter the membrane without electrostatic hindrance of the outermost anion p2mo18. The multilayer film obtained by using polypyrrole to separate p2mo18o626 - can help to obtain a larger catalytic current and make the electrode surface have catalytic ability.