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.
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