The properties of the alcohol-oxidase from yeasts assimilating of methanol(Hansenula polymorpha CBS 4732, Pichia pastoris CBS 2612 and Candida boidinii CBS 8106) as free(cellules, purified enzymes) and immobilized forms(immobilized cellules, immobilized enzymes) were investigated. Immobilization enhanced the activity and stability of alcohol-oxidase to a certain degree. The optimum temperature of the immobilized alcohol-oxidase was lower than those of the free forms. The pH / activi쇼 profiles of alcohol-oxidase did not change by immobilization, but changed by the microorganisms. When the immobilized cellules were stocked at 4$^{circ}C$ in 10mM potassium phosphate buffer(pH 7.5 or 8.0), alcohol-oxidase was more stable than those were stocked in potassium phosphate buffer containing 0.65M sucrose. The immobilization modifies the conditions of oxidation on the various substrates. alcohol-oxidase in immobilized forms showed some with higher Km value for methanol than that in free ones.