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The glucoamylase system of Aspergillus oryzae cultured on wheat bran was separated into 3 active fractions by (NH4)2SO4, rivanol and ethanol precipitation followed by ion exchange chromatography on DEAE‐Sephadex A‐25. One of these fractions, referred to as glucoamylase I was purified by further chromatography on hydroxyapatite gel and Sephadex G‐200. The other two fractions referred to as glucoamylase II and III were purified by further gel filtration on Sephadex G‐200. The purified glucoamylases were found to be homogeneous on 7.5% polyacrylamide gel electrophoresis and isoelectric focusing by carrier ampholites.
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Miah et al. (1977) studied this question.
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