Cereal Chem 46:317 - 324.  |  VIEW ARTICLE
Wheat Proteases. I. Separation and Detection by Starch-Gel Electrophoresis.

E. Kaminski and W. Bushuk. Copyright 1969 by the American Association of Cereal Chemists, Inc. 

A modified starch-gel electrophoresis technique with hemoglobin as substrate was used to study the proteolytic enzymes of the flour from one variety of Canadian HRS wheat. The fractions examined were water-, salt-, 70% ethanol-, and acetic acid-soluble, and six glutens washed out with different solvents. Proteolytically active components were detected in all flour fractions and were classified into four broad groups, A, B, C, and D, on the basis of mobility. The most active group is C which is localized mainly in the alcohol-soluble fraction. This study showed that wheat proteases either are highly heterogeneous or readily associate with other proteins. At low ionic strength, self-digestion occurred in the protein bands which represented the most active groups, C and D.