Cereal Chem 47:140 - 146.  |  VIEW ARTICLE
Properties of Wheat Beta-Amylase Adsorbed on Glutenin.

J. A. Rothfus and S. J. Kennel. Copyright 1970 by the American Association of Cereal Chemists, Inc. 

Incubation of saline-soluble wheat beta-amylase with glutenin produces an insoluble enzymatically active complex. The pH profile of the bound enzyme indicates that binding may be selective for only certain wheat amylases. Association with glutenin reduces enzyme activity, but similarity between the kinetic properties of bound and unbound beta-amylase suggests that binding involves a portion of the enzyme that is remote from its catalytic site. Elevated temperatures increase the activity of bound beta-amylase, but the relation between activity and temperature changes at 20 C. Calculated activation energies are 11.7 kcal./mol. between 4 and 20 C. and 8.8 kcal./mol. between 20 and 55 C. The apparent Michaelis constant for the bound enzyme is 0.15% (w./v.). Little or no active enzyme is released from the complex by disulfide- reducing agents, 0.1M NaCl, or temperatures up to 55 C.