Trust Sanger Institute, Wellcome Trust Genome Campus,. Hinxton, Cambridge ... Medical Genetics,St. George's Hospital Medical School,. Cranmer Terrace ...
Biochemical Society Transactions (2002) Volume 30, Part 6
47 The stability of diet-derived proteins to pepsin digestion and potential allergenicity J.A. Robertson, N.M. Rigby, G. Burnett, A. Fillery-Travis, E.N.C. Mills Physical Biochemistry, Institute of Food Research, Norwich Research Park, Colney, NORWICH, NR4 7UA, UK Resistance to pepsinolysis has been suggested as a predictor for allergenic risk in food proteins. Consequently pepsinolysis has become incorporated into decision tree assessment for potential allergenic risk in novel food systems. Existing methods take little account of interaction between food structure and physiological conditions during digestion in vivo. This problem is being addressed through the development of a more physiologically-based in vitro test digestion system, using a range of proteins; to include common dietary protein and potential allergens. Each has been subjected to controlled pepsinolysis, with associated SDS-PAGE and HPLC analysis. Proteins were digested at 37°C in simulated gastric fluid (pH 2) at selected substrate:pepsin ratios and sampled over a 1 hour time course. SDS-PAGE showed food allergens, eg plactoglobulin and Brazil nut 2s albumin, resisted digestion; similar to haemoglobin. BSA was very susceptible to pepsinolysis, like the potential allergen pcasein. N o accumulation of peptide degradation products was noticed from SDS-PAGE. HPLC gave a range of degradation products (expected MW
