PMID: 2493265Feb 23, 1989Paper

Characterization and localization of the sporulation glucoamylase of Saccharomyces cerevisiae

Biochimica Et Biophysica Acta
T A PughM J Clancy

Abstract

Glucoamylase (SGA) was purified approximately 250-fold from sporulating Saccharomyces cerevisiae cells. The partially purified enzyme was active against glycogen, starch, maltotriose and maltose. It exhibited maximum catalytic activity against glycogen at pH 5.5. The enzyme appears to be glycosylated, because it bound to lentil-lectin Sepharose. SGA was expressed in vegetatively growing cells under the control of the GAL1 promoter, and the cellular location of the enzymatic activity determined by fractionation techniques. SGA was preferentially recovered in fractions which were enriched for the vacuolar hydrolases, carboxypeptidase Y and alpha-mannosidase.

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Citations

Mar 20, 2013·World Journal of Microbiology & Biotechnology·Favaro LorenzoCasella Sergio
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Mar 15, 2020·Applied Microbiology and Biotechnology·Kristoffer Krogerus, Brian Gibson
Jun 1, 1990·Molecular & General Genetics : MGG·T A Pugh, M J Clancy

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