Characterization of two galactosidases extracted from wheat germ with a hydroalcoholic solvent

Abstract α- and β- d -galactosidase were characterized from a hydroalcoholic ectract of wheat germ ( Triticum vulgare ). Kinetic constants ( V max and K M ) and the optimal hydrolysis of p -nitrophenyl galactopyranosides by both enzymes were determined. These enzymes presented a high stability in hydroalcoholic medium and were inhibited by iodoacetamide and sodium p -hydroxymercuribenzoate.