Stability of enzyme inhibitors and lectins in foods and the influence of specific binding interactions.

Abstract

Proteins with actual or potential antinutrient or toxicant activity found in foodstuffs include (1) enzyme inhibitors, especially those specific for serine proteinases and alpha-amylases, and (2) lectins (hemagglutinins). These inhibitors and lectins must be inactivated during processing or food preparation, usually by heat, to avoid possible undesirable effects. Knowledge of their heat stabilities thus helps determine conditions required for their inactivation or denaturation. Many are heat-stable proteins, and their conformations can be stabilized or destabilized by interactions with other constituents present in the food or the digestive tract. Differential scanning calorimetric (DSC) results show that specific binding interactions can lead to substantial increases in kinetic thermal stability of proteins. Examples of such stabilization include serine proteinase-proteinase inhibitor, alpha-amylase-amylase inhibitor, and metal ion-lectin complexes. The extent of thermal stabilization of proteinases in complexes with inhibitors is correlated with the equilibrium association constant. Presence of more than one denaturing unit revealed by DSC in complexes involving multiheaded inhibitors can be interpreted in relation to domain structures of the inhibitors. Basic information on stability of the enzyme inhibitors and lectins is relevant to food processing, quality, and safety.