Proteases of Stored Product Insects and their Inhibition by Specific Protease Inhibitors from Soybeans and Wheat Grain
Abstract
A revised method with high yield for isolation of the labile trypsin- like enzyme from Tenebrio molitor larval midgut has been worked out. A technique using poly-acrylamide gel electrophoresis (PAGE) that includes gelatin as a substrate was successfully employed for the separation and identification of numerous midgut proteases in Tenebrio and Tribolium. The PAGE-gelatin matrix revealed the inhibitory effect of BBI (the proteinaceous trypsin-chymotrypsin inhibitor from soybeans) on several Tribolium proteases - an effect which was not detectable in inhibition assays in solution. The isolation, characterization and kinetic properties of a chymotrypsin-like enzyme from the digestive tract of the locust are described. Comparison of locust chymotrypsin to other chymotrypsins and the effect of inhibitors are discussed.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 31, 1989
- Accession Number
- ADA205264
Entities
People
- Shalom W. Applebaum
- Yehudith Birk
Organizations
- Hebrew University of Jerusalem