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Mar Biotechnol (NY). 2008 Jan-Feb;10(1):75-82. Epub 2007 Oct 13.

Purification and characterization of a cold-adapted alpha-amylase produced by Nocardiopsis sp. 7326 isolated from Prydz Bay, Antarctic.

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1
Key Laboratory of Marine Biogenetic Resources, State Oceanic Administration, Xiamen, PR China.

Abstract

An actinomycete strain 7326 producing cold-adapted alpha-amylase was isolated from the deep sea sediment of Prydz Bay, Antarctic. It was identified as Nocardiopsis based on morphology, 16S rRNA gene sequence analysis, and physiological and biochemical characteristics. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and zymogram activity staining of purified amylase showed a single band equal to a molecular mass of about 55 kDa. The optimal activity temperature of Nocardiopsis sp. 7326 amylase was 35 degrees C, and the activity decreased dramatically at temperatures above 45 degrees C. The enzyme was stable between pH 5 and 10, and exhibited a maximal activity at pH 8.0. Ca(2+), Mn(2+), Mg(2+), Cu(2+), and Co(2+) stimulated the activity of the enzyme significantly, and Rb(2+), Hg(2+), and EDTA inhibited the activity. The hydrolysates of soluble starch by the enzyme were mainly glucose, maltose, and maltotriose. This is the first report on the isolation and characterization of cold-adapted amylase from Nocardiopsis sp.

PMID:
17934774
DOI:
10.1007/s10126-007-9035-z
[Indexed for MEDLINE]
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