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Cereal Chem 58:433 - 437.  |  VIEW ARTICLE
Pearl Millet Amylases. I. Properties of Partially Purified Alpha-Amylase.

A. Beleia and E. Varriano-Marston. Copyright 1981 by the American Association of Cereal Chemists, Inc. 

The purification method affected the physicochemical characteristics of purified millet alpha-amylases. Polyacrylamide gel electrophoresis showed three protein bands for alpha-amylase purified by glycogen complex formation and seven for alpha-amylase purified by starch column procedures. All protein bands exhibited alpha-amylase activity. Alpha-amylase isozymes had molecular weights, determined by sodium dodecyl sulfate gel electrophoresis, ranging from 22,000 to 53,000 and isoelectric points ranging from 4.8 to 6.2. The pH optima were between 4.4 and 4.8; temperature optimum was 55 C. Many of the above characteristics are similar to those reported for amylases purified from immature cereal grains.

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