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. 1977 Oct;34(4):391–397. doi: 10.1128/aem.34.4.391-397.1977

Production, purification, and characterization of alpha-amylase from Thermomonospora curvata.

J L Glymph, F J Stutzenberger
PMCID: PMC242669  PMID: 21612

Abstract

Thermomonospora curvata produces an extracellular alpha-amylase. Maximal amylase production by cultures in a starch-mineral salts medium occurred at pH 7.5 and 53 degrees C. The crude enzyme was unstable to heating (65 degrees C) at pH 4 to 6, and was activated when heated at pH 8. The enzyme was purified 66-fold with a 9% yield and appeared homogeneous on discontinuous gel electrophoresis. The pH and temperature optima for activity of the purified enzyme were 5.5 to 6.0 and 65 degrees C. The molecular weight was calculated to be 62,000. The Km for starch was 0.39 mg/ml. The amylolytic pattern consisted of a mixture of maltotetraose and maltopentaose.

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Selected References

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