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. 1979 Oct;38(4):616–620. doi: 10.1128/aem.38.4.616-620.1979

Purification and Some Properties of an Extracellular Amylase from a Moderate Halophile, Micrococcus halobius

Hiroshi Onishi 1, Koji Sonoda 1
PMCID: PMC243549  PMID: 16345444

Abstract

A moderate halophile, Micrococcus halobius ATCC 21727, produced an extracellular dextrinogenic amylase when cultivated in media containing 1 to 3 M NaCl. The amylase was purified from the culture filtrate to an electrophoretically homogenous state by glycogen-complex formation, diethylaminoethyl-cellulose chromatography, and Bio-Gel P-200 gel filtration. The enzyme had maximal activity at pH 6 to 7 in 0.25 M NaCl or 0.75 M KCl at 50 to 55°C. The activity was lost by dialysis against distilled water. Molecular weight was estimated to be 89,000 by sodium dodecyl sulfate-gel electrophoresis. The action pattern on amylose, soluble starch, and glycogen showed that the products were maltose, maltotriose, and maltotetraose, with lesser amount of glucose.

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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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