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. 1976 Nov;128(2):515–521. doi: 10.1128/jb.128.2.515-521.1976

Stable, inducible thermoacidophilic alpha-amylase from Bacillus acidocaldarius.

V Buonocore, C Caporale, M De Rosa, A Gambacorta
PMCID: PMC232785  PMID: 10276

Abstract

Bacillus acidocaldarius Agnano 101 produces an inducible thermoacidophilic alpha-amylase. The enzyme production occurs during the stationary phase of growth in the presence of compounds with alpha-1,4-glucosidic linkages. The enzymatic activity is both present in the culture medium and associated with the cells; the enzymes purified from both sources show identical molecular and catalytic properties. The purified amylase has a single polypeptide chain of molecular weight 68,000 and behaves like an alpha-amylase with affinity constants for starch and related substances of 0.8 to 0.9 mg/ml. The pH and temperature optima for activity are 3.5 and 75degreesC, respectively. The amylase is stable at acidic pH (below 4.5). Its thermal stability is strictly dependent upon protein concentration; the half-life at 60degreesC of the amylase in a 70-mug/ml solution is about 5 days.

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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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