The effects of reaction temperature and the level of hydration(water activity) were studied for gas phase reactions of alcohol oxidase and alcohol dehydrogenase immobilized on DEAE-cellulose and controlled pore glass(CPG). Optimum reaction temperature zone of gas phase reaction was similar to that of aqueous phase reaction. The activity of alcohol oxidase increased dramatically and the stability decreased when the water activity was increased from 0.3 to 0.8. The apparent activation energies of the gas phase reaction decreased approaching the values obtained in the aqueous phase reaction as the water activity increased. In the both case of alcohol oxidase and alcohol dehydrogenase, the rate constants of the gas phase reaction were lower than those of aqueous phase reaction by two orders of magnitude and these results could be correlated to the vapor-liquid equilibrium data of the substrate, ethanol.