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. 1982 Dec;44(6):1253–1257. doi: 10.1128/aem.44.6.1253-1257.1982

Extracellular Isoamylase Produced by the Yeast Lipomyces kononenkoae

Isabel Spencer-Martins 1
PMCID: PMC242182  PMID: 16346143

Abstract

A strain of the starch-converting yeast Lipomyces kononenkoae produced, when grown on starch, a debranching enzyme that proved to be an isoamylase (glycogen 6-glucanohydrolase; E.C. 3.2.1.68). So far, only bacteria have been found to produce extracellular isoamylases. The yeast isoamylase enhanced β-amylolysis of amylopectin and glycogen and completely hydrolyzed these substrates into maltose when combined with a β-amylase but had no action on dextran or pullulan. By isopropanol precipitation and carboxymethyl cellulose chromatography, L. kononenkoae isoamylase was partially purified from the supernatant of cultures grown on a mineral medium with soluble starch. Optimum temperature and pH for activity of the isoamylase were 30°C and 5.6. The molecular weight was around 65,000, and the pI was at pH 4.7 to 4.8. The Km (30°C, pH 5.5) for soluble starch was 9 g liter−1.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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