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The immune response of wheat flour modified by the treatment with subtilisin under different conditions of temperature, incubation periods and the ratio of enzyme/wheat flour was investigated. Respective protein fractions, namely, albumins, globulins, gliadins and glutenins were obtained from the modified wheat flour on the basis of their diverse solubility. The particular wheat protein fractions were examined for the immune reaction by the use of an indirect non-competitive ELISA method. Commercially available antibodies, namely, monoclonal anti-human IgG and monoclonal anti-human IgE conjugates with alkaline phosphatase and human sera with elevated IgG as well as rabbit sera against QQQPP peptide were tested. The highest decrease in gliadins immunoreactivity was observed for wheat flour modified under following conditions: temperature 37°C, 18 h of incubation time and the enzyme/wheat flour ratio of 1:10 000.
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p.335-340,fig.,ref.
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- Technical University of Lodz, Stefanowskiego 4/10, 90-924 Lodz, Poland
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Bibliografia
- 1. Aalberse R.C., Food allergens. Environ. Toxicol. Pharmacol., 1997, 4, 55–60.
- 2. Besler M., Steinhart H., Paschke A., Stability of food allergens and allergenicity of processed foods. J. Chromatogr. B, 2001, 756, 207–228.
- 3. Bevan S., Popat S., Houlston R.S., Relative power of linkage and transmission disequilibrium test strategies to detect non‑HLA linked coeliac disease susceptibility genes. Gut, 1999, 45, 668–671.
- 4. Catassi C., Ratsch I.M., Fabiani E., Rossini M., Bordicchia F., Candela F., Coppa G.V., Giorgi P.L., Coeliac disease in the year 2000: Exploring the iceberg. Lancet, 1994, 343, 200–203.
- 5. Chapman M.D., Smith A.M., Vailes L.D., Arruda L.K., Dhanaraj V., Pomes A., Recombinant allergens for diagnosis and therapy of allergic disease. J. Allergy Clin. Immunol., 2000, 106, 409–418.
- 6. Clemente A., Vioque J., Sanchez-Vioque R., Pedroche J., Millan F., Production of extensive chickpea (Cicer arietinum L.) protein hydrolysates with reduced antigenic activity. J. Agric. Food Chem., 1999, 47, 3776–3781.
- 7. Denery-Pappini S., Nicols Y., Popineau Y., Efficiency and limitations of immunochemical assays for the testing of gluten-free foods. J. Cereal Sci., 1999, 30, 121–131.
- 8. Dohi M., Suko M., Sugiyama H., Yamashita N., Tadokoro K., Juji F., Okudaira H., Sano Y., Ito K., Miyamoto T., Food-dependent, exercise-induced anaphylaxis: a study on 11 Japanese cases. J. Allergy. Clin. Immunol., 1991, 87, 34–40.
- 9. Estaban M.M., Adverse reactions to foods in infancy and childhood. J. Pediatr., 1992, 121, 1–126.
- 10. Hughes D.A., Mills C., Food allergy: a problem on the increase. Biologist, 2001, 48, 201–205.
- 11. Leszczyńska J., Łącka A., Pytasz U., Szemraj J., Lukamowicz J., Lewiński A., The effect of proteolysis on the gliadin immunoreactivity. Pol. J. Food Nutr. Sci., 2002, 11, SI 2, 145–148.
- 12. Leszczynska J., Łącka A., Bryszewska M., Brzezińska-Błaszczyk E., The usefulness of rabbit anti-QQQPP peptide antibodies to wheat flour antigenicity studies. Czech. J. Food Sci., 2008, 26, 24–30.
- 13. Osborne T.B., The proteins of the wheat kernel. 1907, Carnegie Institute, Washington DC, Publ. No.84.
- 14. Rao M.B., Tanksale A.M., Ghatge M.S., Desphande V.V., Molecular and biotechnological aspects of microbial proteases. Microbiol. Mol. Biol. Rev., 1998, 62, 597–635.
- 15. Restani P., Plebani A., Velonà T., Cavagni G., Ugazio A.G., Poiesi C., Muraro A., Galli C.L., Use of immunoblotting and monoclonal antibodies to evaluate the residual antigenic activity of milk protein hydrolysed formulae. Clin. Exp. Allergy, 1996, 26, 1182–1187.
- 16. Rumbo J., Chirdo F.G., Fossati C.A., Anon M.C., Influence of thermal treatment of food on the immunochemical quantification of gliadin. Food. Agric. Immunol., 1996, 8, 195–203.
- 17. Santos J., Bayarri C., Saperas E., Nogueiras C., Antolin M., Mourella M., Cadahia A., Malagelada J.R., Characterisation of immune mediator release during the immediate response to segmental mucosal challenge in the jejunum of patients with food allergy. Gut, 1999, 45, 553–558.
- 18. Skerritt J.H., Devery J.M., Hill A.S., Gluten intolerance: Chemistry, celiac-toxicity, and detection of prolamins in foods. Cereal Foods World, 1990, 35, 638–644.
- 19. Tanabe S., Arai S., Yanagihara Y., Mita H., Takahashi K., Watanabe M., A major wheat allergen has a Gln-Gln-Gln-Pro-Pro motif identified as an IgE-binding epitope. Biochem. Biophys. Res. Commun., 1996, 219, 290–293.
- 20. Van Eckert R., Scharf M., Wald T., Pfanhauser W., Determination of protein with ELISA-methods: doubtful quantitative results? 1997, in: Proceedings of Euro Food Chem IX, vol. 1, 24-26 September 1997, Interlaken, Switzerland, p. 354.
- 21. Vioque J., Sanchez-Vioque R., Clemente A., Pedroche J., Millan F., Partially hydrolyzed rapeseed protein isolates with improved functional properties. J. Am. Oil Chem. Soc., 2000, 77, 447–450.
- 22. Walsh B.J., Howden M.E., A method for the detection of IgE binding sequences of allergens based on a modification of epitope mapping. J. Immunol. Methods, 1989, 121, 275–280.
- 23. Weiss W., Vogelmeier C., Görg A., Electrophoretic characterization of wheat grain allergens from different cultivars involved in baker’s asthma. Electrophoresis, 1993, 14, 805–816.
- 24. Weiss W., Huber G., Engel K.H., Pethran A., Dunn M.J., Gooley A.A., Görg, A., Identification and characterization of wheat grain albumin/globulin allergens. Electrophoresis, 1997, 18, 826–833.
- 25. Wieser H., Comparative investigations of gluten proteins from different wheat species. III. N-terminal amino acid sequences of alpha-gliadins potentially toxic for coeliac patients. Eur. Food Res. Technol., 2001, 213, 183–186.
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Bibliografia
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