Cereal Chem 49:580 - 585. | VIEW
The Isoelectric Focusing Electrophoresis of Wheat Beta-Amylases.
M.-L. Niku-Paavola, M. Nummi, A. Kachkin, J. Daussant, and T.-M. Enari. Copyright 1972 by the American Association of Cereal Chemists, Inc.
The different forms of wheat beta-amylase---free and bound beta-amylase from mature wheat and beta- amylase from germinated wheat---are analyzed by means of isoelectric focusing electrophoresis. The results demonstrate the heterogeneity of wheat beta-amylases; the free enzyme has isoelectric points at pH values of 4.8, 4.9, 5.6, and 5.8. After storage of wheat extracts, only the components at pH 4.8 and 4.9 are left. By fractionation with ammonium sulfate precipitation, free enzyme can be purified as two components: one with pI 4.8 and 4.9, and the other with pI 5.8. The bound enzyme is almost homogeneous; its pI is 5.0. The beta-amylase from germinated wheat has pI values of 5.5 and 5.8. The results suggest that the base structure of the different components is the same.