Author's Organization:Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
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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