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Purification and Properties of Amylases Extracellularly Produced by an Imperfect Fungus, Fusidium sp. BX-1 in a
1a Department of Bioproduction Science, Faculty of Horticulture , Chiba University , Matsudo , Matsudo-shi , Chiba 271, Japan.
Abstract:
Amylases (I and II) extracellularly produced by an imperfect fungus, Fusidium sp. BX-1 in a medium containing glycerol as a carbon source, were purified as electrophoretically and isoelectrophoretically homogeneous proteins. The electrophoretical mobilities of amylase I and II on native and SDS-polyacrylamide gels exactly coincided with each other. Their molecular weights were estimated to be about 52,000. The sugar contents of amylase I and II were 3.4 and 4.7%, and the pIs were 8.70 and 8.55, respectively. The Kms of the enzymes for soluble starch were 0.053 and 0.044%. The actions of the enzymes on soluble starch, short chain amyloses, and maltose were examined. Amylase I and II are identified as being to an α-amylase and a glucoamylase, respectively.
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