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ISOLATION AND CHARACTERISATION OF THE AMYLOTIC SYSTEM OF SCHWANNIOMYCES CASTELLII
Author(s) -
Sills A. M.,
Sauder M. E.,
Stewart G. G.
Publication year - 1984
Publication title -
journal of the institute of brewing
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.523
H-Index - 51
eISSN - 2050-0416
pISSN - 0046-9750
DOI - 10.1002/j.2050-0416.1984.tb04281.x
Subject(s) - maltose , isomaltose , chemistry , amylase , hydrolysis , starch , enzyme , chromatography , biochemistry , substrate (aquarium) , biology , ecology
The amylolytic system of Schwanniomyces castellii has been isolated and purified by means of ultrafiltration followed by polyacrylamide gel electrophoresis. Both α‐amylase and glucoamylase were purified. α‐Amylase activity was stable from pH 5·5 to 6·5 and glucoamylase activity was stable at a more acidic range of pH 4·2 to 5·5. The optimal temperature of α‐amylase activity was between 30 and 40°C with rapid deactivation at 70°C. The optimal temperature of glucoamylase was 40 to 50°C with rapid decline of activity at 60°C. The K m of α‐amylase with soluble starch as the substrate was 1·15 mg/ml and the K m of glucoamylase with the same substrate was 10·31 mg/ml. Glucoamylase was able to hydrolyze α‐1, 4 and α‐1,6 glucosidic linkages, as demonstrated by its ability to hydrolyse maltose and isomaltose respectively, whereas α‐amylase could hydrolyse α‐1,4 glucosidic linkages only. α‐Amylase was shown to be a glycoprotein, whereas no carbohydrates were associated with glucoamylase.