Proteases of Stored Product Insects and Their Inhibition by Specific Protease Inhibitors from Soybeans and Wheat Grain
Abstract
Trypsin-like and chymotrypsin-like enzymes have been identified and separated from the digestive tracts of three model insects: the rust red flour beetle Tribolium castaneum, the mealworm Tenebrio molitor and the locust Locusta migratoria. These trypsins and chymotrypsins from legume seeds, such as the Bowman-Birk inhibitor (BBI) from soybeans and CI from chickpeas. The purified and partially-characterized insect trypsins and chymotrypsins differ significantly from the respective mammalian enzymes in their low content of sulfur-containing amino acids in general and complete lack of disulfide bridges in particular. This suggests a different three-dimensional structure and assembly of the insect digestive proteases. A revised method with high yield for isolation of the labile trypsin-like and chymotrypsin-like enzymes from Tenebrio molitor larval midgut has been worked out. The method is based on affinity chromatography separation on immobilized, synthetic specific inhibitors which have a very low affinity for the respective enzymes in solution. Keywords: Enzyme inhibitors, Peptide hydrolases.
Document Details
- Document Type
- Technical Report
- Publication Date
- Dec 15, 1989
- Accession Number
- ADA218034
Entities
People
- Shalom W. Applebaum
- Yehudith Birk
Organizations
- Hebrew University of Jerusalem