Digestion of Allergenic Fragments of Gliadin by Purified Enzymes from Hepatopancreas of Palinurus Elephas (Fabricius, 1787)

Abstract

Viscera from marine organisms are rich potential sources of various enzymes that may have some unique properties of interest for both basic research and industrial applications. Main digestive proteinases detected in the hepatopancreas of marine organism are trypsin and chymotrypsin (Kishimura H et al., Food Chemistry, 2006). High activity of fish enzymes at low temperatures is interesting for industrial applications, especially in certain food processing. One application is the hydrolysis of protein resistant to gastrointestinal digestion like Coeliac disease. In this work enzymes extracted and partially purified proteases from hepatopancreas from Palinurus elephas are analyzed. Moreover, using human Celiac Serum in immunoblotting analyses, we observed that immunological epitope of gliadin, normally recognized from IgE immunoglobulin, disappear after digestion after digestion of gliadin with purified enzyme. These data strongly suggest that, in the partially purified enzymes by hepatopancreas, are present specific proline enzymes.