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Glucose was the only product of starch hydrolysis liberated by glucoamylase. The enzyme was a glycoprotein with an isoelectric point at pH 3·4 and was optimally active at pH 4·0 and 60°C. It was remarkably stable over a wide range of pH and at elevated temperatures. Divalent Mg 2+ ’and Ca 2+ slightly stimulated glucoamylase activity. The enzyme exhibited specificity for substrates containing α(1 → 4) glucosidic linkages and the Km for starch hydrolysis was 4·0 g/l.
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Ali et al. (1991) studied this question.
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