Immobilization of Invertase in Copolymer of 2,5-Di(thiophen-2-yl)-1-p-Tolyl-1H-Pyrrole with Pyrrole

Abstract

Immobilization of invertase in conducting copolymer matrix of 2,5-di(thiophen-2-yl)-1-p-tolyl-1H-pyrrole with pyrrole (poly(DDTPco-Py)) was achieved via electrochemical polymerization. Kinetic parameters, Michaelis-Menten constant, K m and the maximum reaction rate, V max were investigated. Operational stability and temperature optimization of the enzyme electrodes were also examined.Immobilized invertase reveals maximum activity at 50 • C and; pH 8 and pH 4 for two copolymer matrices. Although the same two monomers are utilized for the copolymer synthesis, the way the copolymer is produced results in quite different responses in terms of enzyme activity, optimum pH and kinetic parameters. Excellent operational stability of the enzyme electrodes enables their repetitive use in the determination of invert sugar.

Enzyme immobilization in a photosensitive conducting polymer bearing azobenzene in the main chain

“…The decrease in the reaction rate, which was observed for immobilized enzyme in PPy matrix with respect to free one might be resulted from the difficulty in diffusion of substrate to the matrix as compared to diffusion in solution. In Table 1, kinetic parameters of different invertase sensors which have already been reported [24][25][26][27], can be seen to be able to compare with these values of the P(TDAZO-co-Py)/invertase electrode.…”