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Purification and characterization of the extracellular glucoamylase from the yeast Trichosporon adeninovorans

✍ Scribed by R. Büttner; Dr. R. Bode; D. Birnbaum

Publisher
John Wiley and Sons
Year
1987
Tongue
English
Weight
581 KB
Volume
27
Category
Article
ISSN
0233-111X

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✦ Synopsis

The yeast Trichosporon adeninovorans secretes an amylase a t a high rate if grown in a medium containing starch or maltose. The enzyme was purified 29-fold by hydroxylapatite chromatography and gel filtration and characterized as a glucoamylase. The enzyme seems to be a glycoprotein with a molecular weight of 225,000. The optimal temperature for the glucoamylase activity was 60 to 70 "C in dependence on the substrate concentration. The enzyme displayed highest activity in a pH range of 4.0-5.5. I n the absence of starch or maltose the thermal stability was low but in the presence of substrate a rapid increase of the enzyme stability was observed. The K , values of the enzyme were estimated t o be 1.2 g/l for soluble starch and 4 g/l for maltose.

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