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J. Biochem, 1974, Vol. 76, No. 6 1365-1367
© 1974 Japanese Biochemical Society

research-article

Transient Kinetics of Gloucoamylase1-catalyzed Hydrolysis of Maltodextrin Studied by the Fluorescence Stopped-flow Method,2

Keitaro HIROMI, Masatake OHNISHI and Takashi YAMASHITA

Department of Food Science and Technology, Faculty of Agriculture, Kyoto University Sakyo-ku, Kyoto, Kyoto 606

The transient phase of the hydrolysis of maltodextrin (with an average degree of polymerization of about 11) catalyzed by glucoamylase [EC 3.2.1.3 [EC] ] from Rhizopus niveus was studied kinetically using a fluorescence stopped-flow method. Rapid decrease in enzyme fluorescence intensity was observed upon mixing the enzyme and substrate solutions, with slow recovery of fluorescence as the overall reaction proceeded. The two phases were concluded to represent formation of an enzyme-substrate complex and recovery of free enzyme on breakdown of the complex into its products.

1{alpha}-1,4 : 1,6-Glucan4 : 6-glucohydrolase, [EC 3.2.1.3 [EC] ].

2This study was supported in part by a grant-in-aid for scientific research from the Ministry of Education.


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