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

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....

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Bibliographic Details
Published in:Biochemical journal 1988, Vol.249 (1), p.163-170
Main Authors: Kleinman, M.J, Wilkinson, A.E, Wright, I.P, Evans, I.H, Bevan, E.A
Format: Article
Language:English
Subjects:
alpha-glucosidase
Amino Acids - analysis
amylases
Aspergillus oryzae - enzymology
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
enzyme activity
Glucan 1,4-alpha-Glucosidase - antagonists & inhibitors
Glucan 1,4-alpha-Glucosidase - isolation & purification
Glucan 1,4-alpha-Glucosidase - metabolism
Glucosidases - isolation & purification
Half-Life
Isoelectric Focusing
Kinetics
Rhizopus - enzymology
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Substrate Specificity
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Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2490163