Properties of wheat beta-amylase adsorbed on glutenin
1970
Incubation of saline-soluble wheat β-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 β-amylase suggests that binding involves a portion of the enzyme that is remote from its catalytic site. Elevated temp. increase the activity of bound β-amylase, but the relation between activity and temp. changes at 20°C. Calculated activation energies are 11.7 kcal/mole between 4° and 20°C, and 8.8 kcal/mole 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 disulphide-reducing agents, 0.1M NaCl, or temp. ≤55°C.
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