The extracellular glucoamylase from certain strains of Saccharomyces cerevisiae can be purified from culture medium by a simple chromatographic procedure. The native enzyme is heavily glycosylated and has an Mr of about 250,000, but gel filtration indicates the existence of oligomers of larger size. Dissociation yields a form of Mr about 70,000. The glucoamylase is rich in serine and threonine and in aspartic acid plus asparagine, and has a pI of 4.62 and a pH optimum of 4.5-6.5. The thermostability and resistance to denaturants of the yeast enzyme is compared with those of two other fungal glucoamylases. Kinetic data for the yeast enzyme and a variety of substrates is presented; the enzyme is particularly ineffective in cleaving alpha-(1—6)-glycosidic bonds.
Purification and properties of an extracellular glucoamylase from a diastatic strain of Saccharomyces cerevisiae
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M J Kleinman, A E Wilkinson, I P Wright, I H Evans, E A Bevan; Purification and properties of an extracellular glucoamylase from a diastatic strain of Saccharomyces cerevisiae. Biochem J 1 January 1988; 249 (1): 163–170. doi: https://doi.org/10.1042/bj2490163
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