特にAspergillus cinnamomeusの生デン粉糖化活性について(糸状菌のアミラーゼに関する研究-3-)

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Amylase systems of Aspergillus cinnamomeus IMA 2040 and its mutant No. 12111, selected by repeated UV irradiations, were known to be composed of 4 components i. e. α-amylase, acid stable α-amylase and glucoamylase I and II. By using DEAE-Sephadex column chromatography, each component was isolated and purified. The activity of total α-amylase produced by the mutant strain was nearly equal with the parent strain, whereas acid stable α-amylase and glucoamylase of the mutant were observed to be 10_??_20 times stronger than the respective enzymes of the parent strain. As for the activity of raw starch saccharification, glucoamylase II was six times stronger than glucoamylase I and α-amylases including crystalline bacterial liquefying amylase were known to be fairly inactive. The molecular weight found by Sephadex G-75 gel filtration chromatography was 45, 000_??_75, 000 for each of the four amylases.
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