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. 1988 Jan 1;249(1):163–170. doi: 10.1042/bj2490163

Purification and properties of an extracellular glucoamylase from a diastatic strain of Saccharomyces cerevisiae.

M J Kleinman 1, A E Wilkinson 1, I P Wright 1, I H Evans 1, E A Bevan 1
PMCID: PMC1148680  PMID: 3124820

Abstract

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.

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Selected References

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