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KMID : 0380219940270060576
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 6 p.576 ~ p.578
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An Improved Method for the Purification of a-Amylase by Affinity Chromatography
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Abstract
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Abstract:
@EN An affinity chromatographic method for the efficient purification of a-amylase expressed from the Bacillus a-amylase gene in Escherichia coli is described, a-Amylase was bound to a starch-iodine complex column while other contaminating
proteins
were
eluted with a binding buffer containing a low concentration of sodium chloride. The attached α-amylase was eluted by changing the pH of the buffer with a high concentration of sodium chloride (1 M) in the buffer. The purified enzyme showed a
single
polypeptide band on SDS gel electrophoresis, and the binding capacity of starch to the α-amylase present in the column was 5696 U/g of starch.
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KEYWORD
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