The responses of a cryohydrogel tyrosinase enzyme electrode to four substrates in three pure water immiscible organic solvents were investigated. Kinetic parameters, the maximum kinetic current, I-max, the apparent Michaelis-Menten constant, K-m(app), and I-max/K-m(app), were calculated. The I-max/K-m(app) value was taken as an indicator of the catalytic efficiency of the sensor. The effect of the substrate hydrophobicity on I-max/K-m(app) and response time of the sensor were discussed. The effects of both hydrophobicity (log P) and dielectric constant (epsilon) of the organic solvent on the catalytic efficiency of the enzyme in the organic phase were studied.