Abstract
Acid-stable (KAA) and neutral (KNA) α-amylases from shochu koji (A. kawachii) were purified and their actions towards maltooligosaccharides were studied. KAA could be distinguished from KNA by the following actions: with KAA, maltopentaose (G5) was preferentially hydrolyzed at the third glycoside bond, and the addition of potassium thiocyanate (KSCN) decreased the rate of CNP-release from 2-chloro-4-nitrophenyl-α-maltotrioside (CNP-G3).
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