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Specificity of Crystalline Saccharogenic Amylase of Moulds


AMONG the saccharogenic amylases of moulds hitherto reported, γ-amylase of Aspergillus awamori Kitahara 1, gluc-amylase of Rhizopus delemar 2 and taka amylase B of Aspergillus oryzae 3 seem to be the most characteristic in their mode of hydrolysing starch. All these amylases, belonging to the group of amylo-(1.4)-glucosidases suggested by Schubert4, have already been purified to a certain degree and reported as being able to split glucose directly from starch, γ-Amylase, however, has been known to leave a limit dextrin when it acts on amylopectin and to show no maltase activity. Gluc-amylase has been reported to hydrolyse soluble starch in such way that with the iodine colour test of the reaction mixture the blue colour still remains even after the starch, calculated as glucose, is more than 90 per cent hydrolysed. The enzyme has also been found to hydrolyse amylopectin almost completely to glucose and to exhibit maltase activity. Taka amylase B on the other hand, has been reported as being similar to γ-amylase hi the hydrolysis of amylopectin, but exhibiting maltase activity.

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    Kitahara, K., and Kurushima, M., J. Ferment. Tech. (Japan), 27, 254 (1949); Mem. Res. Inst. Food Sci., Kyoto Univ., 3, 15 (1952).

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    Schubert, E., Melliand Text. Acta, No. 8, 1 (1954).

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