Abstract
Two enzymes which are concerned with maltose hydrolysis in molds, saccharogenic amylase and maltase, were fractionated by adsorption with calcium triphosphate and elution with potassium-diphosphate and diammoniumphosphate solutions. Maltase was crystallized from diammonium-phosphate eluate by a method involving fractionation with ethanol and acetone, and the removal of salted-out inpurities. It was found that the crystalline maltase hydrolyzes maltose and phenol-α-glucoside but methyl-α-glucoside is not appreciably hydrolyzed, while saccharogenic amylase is inactive toward the latter two substrates. Optimal pH of crystalline maltasc is 3.4 and opt. temperature 50°C.
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