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

2009-01-01
Celebi, Selin
Ibibikcan, Esin
Kayahan, Senem
Yigitsoy, Basak
Toppare, Levent Kamil
Immobilization of invertase in conducting copolymer matrix of 2,5-di(thiophen-2-yl)-1-p-tolyl-1H-pyrrole with pyrrole (poly(DDTP-co-Py)) was achieved via electrochemical polymerization. Kinetic parameters, Michaelis-Menten constant, Km and the maximum reaction rate, Vmax were investigated. Operational stability and temperature optimization of the enzyme electrodes were also examined. Immobilized invertase reveals maximum activity at 50 degrees 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.