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Purification of a-amylase from germinating little millets (Panicum sumatrense)

Author(s): B. Usha and K. P. J. Hemalatha*

Journal: Journal of Pharmacy Research
ISSN 0974-6943

Volume: 4;
Issue: 5;
Start page: 1370;
Date: 2011;
Original page

Keywords: a-amylase | little millet | purification | properties | Panicum sumatrense

The crude extract of a-amylase (alpha 1-4D-glucan glucanohydrolase EC was obtained from little millet (Panicum sumatrense L. Roth ex Roem. et Schult.) cotyledons excised from 3-day-old seedlings. The activity of a-amylase increased dramatically both in specific activity and total activity on day 3 when germination occurs in the dark. The enzyme was purified 10.15 fold with a five-step procedure including homogenization, acetone precipitation, ammonium sulfate fractionation, ion-exchange chromatography on DEAE cellulose, gel permeation chromatography on Sephadex G-150. The amylase purified was a monomer with molecular weight 46 kDa, which optimally hydrolyzes soluble starch at a temperature of 50°C and pH 5.0. The Michaelis constant for the enzyme catalyzed reaction (Km) is 1.6 mg soluble starch/ml.
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