Abstract
α-Amylase accumulated in the growth medium of the yeast Lipomyces starkeyi (NCYC 1436) to a maximum of 12 units ml−1 after 15 days' batch culture in a soluble starch medium. Extra α-amylase activity, about 50% of that released into the medium, could be extracted from the cells by a salt wash. α-Amylase was purified by salt precipitation followed by ion exchange chromatography and gel filtration. Native gel electrophoretic analysis showed the presence of three distinct amylolytic enzymes, with molecular weights of approximately 50, 70 and 80 kDa.
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