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Cereal Chem 59:351 - 355.  |  VIEW ARTICLE
Amylolysis of Pearl Millet Starch and Its Fractions by Pearl Millet Alpha-Amylase.

S. Abdul-Hussain and E. Varriano-Marston. Copyright 1982 by the American Association of Cereal Chemists, Inc. 

Alpha-amylase was isolated from germinated pearl millet and purified by glycogen-amylase complex formation. Germination resulted in a 120-fold increase in specific activity of the enzyme over that of alpha- amylase from mature grain. Amylolysis of millet starch and its fractions by purified alpha-amylase was studied by gel filtration. Raw millet starch was resistant to attack by alpha-amylase from germinated millet. Only limited degradation (26%) occurred after starch was incubated with the enzyme for 24 hr at 35 C. Millet amylose was readily hydrolyzed by purified millet alpha-amylase. During a 10-min reaction period at 35 C, 36% of the molecule was degraded to molecular weights of 40,000-10,000. Conversely, some portions of millet amylopectin were hydrolyzed slowly by alpha-amylase.

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