Enzymatic Modification of Glucoamylase of Aspergillus awamori var. kawachi

概要

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Glucoamylase (GA) of Aspergillus awamori var. kawachi was found to consist of three types, I, I' and II. On incubation with the commercial enzyme preparation "Pronase", GA I (MW 90,000; N-terminal alanine; raw starch-digestible) was converted to two other types of GA, one identical with GA I' (MW 83,000; N-terminal alanine plus isoleucine; no activity toward raw starch), the other identical with GA II (MW 57,000; N-terminal isoleucine; no activity toward raw starch) in the hydrolysis curves for gelatinized potato starch and glysogen, pH- and thermo-stabilities, molecular weight and N-terminal amino acids. The incubatin of GA I with Turbo-glycosidases resulted in liberation of 70% of its carbohydrate moiery. The GA prodyced by this treatment (MW 84,000; N-terminal alanine) had similar low stability to GA II, but was identical with GA I in the hydrolysis modes on various substrates. This enzyme was converted by the fungal acid protease to another type of GA (MW 57,000; N-terminal isoleucine), which exhibited the same hydrolysis curves and stabilities as GA II. The limited stepwise degradations of GA I with gungal acid protease and glycosidases resulted in the occurrence of multiple forms of GA, similar to those observed in cultures of A. awamori var. kawachi.
公益社団法人日本生物工学会の論文
1978-08-25