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Vol. 140, No. 1, 2006
Issue release date: April 2006
Int Arch Allergy Immunol 2006;140:36–42

Profile Analysis and Immunoglobulin E Reactivity of Wheat Protein Hydrolysates

Akiyama H. · Sakata K. · Yoshioka Y. · Murata Y. · Ishihara Y. · Teshima R. · Sawada J. · Maitani T.
aDivision of Foods and bDivision of Biochemistry and Immunochemistry, National Institute of Health Sciences, cKyowa Hakko Food Specialties Co., Ltd., and dMaruha Group Inc., Tokyo, Japan

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Background: Wheat protein hydrolysates have been traditionally used as food additives and are now being used in cooking worldwide. There have been a few studies on the relationship between the molecular mass distribution and the immunoglobulin E (IgE) reactivity of the wheat protein hydrolysates. Method: We analyzed the peptide profile of commercial wheat protein hydrolysate samples from enzymatic or acid hydrolysis of wheat protein using size exclusion chromatography. We further investigated the IgE reactivity of the wheat protein hydrolysates using the inhibition ELISA method and sera of 5 patients sensitive to wheat. Results: The wheat protein enzymatic hydrolysate samples showed high concentrations of peptides with molecular masses greater than 1,050 Da, whereas in contrast, the wheat protein acid hydrolysates showed extremely low concentrations of peptides with molecular masses greater than 1,050 Da. Tested wheat protein acid hydrolysates hardly inhibited the patient IgE binding ability to wheat proteins in the five patient sera. On the contrary, some tested wheat protein enzymatic hydrolysate samples inhibited the IgE binding ability to wheat proteins. Conclusion: These results suggested that the uptake of wheat protein enzymatic hydrolysates might still have the possibility of causing food allergic reactions in patients allergic to wheat and the processed foods containing them.

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  1. Sampson HA: Update on food allergy. J Allergy Clin Immunol 2004;113: 805–819.
  2. Maruyama N, Ichise K, Katsube T, Kishimoto T, Kawase S, Matsumura Y, Takeuchi Y, Sawada T, Utsumi S: Identification of major wheat allergens by means of the Escherichia coli expression system. Eur J Biochem 1998;255:739–745.
  3. Palosuo K, Alenius H, Varjonen E, Koivuluhta M, Mikkola J, Keskinen H, Kalkkinen N, Reunala T: A novel wheat gliadin as a cause of exercise-induced anaphylaxis. J Allergy Clin Immunol 1999;103:912–917.
  4. Shewry PR, Tatham A S: The prolamin storage proteins of cereal seeds: structure and evolution. Biochem J 1990;267:1–12.
  5. Tanabe S, Arai S, Watanabe M: Modification of wheat flour with bromelain and baking hypoallergenic bread with added ingredients. Biosci Biotechnol Biochem 1996;60:1269–1272.
  6. Ikezawa Z, Tsubaki K, Yokota S: Effect of hypoallergenic wheat (HAW-A1) on atopic dermatitis (AD) with wheat allergy, and its antigenic analysis using sera from patients with AD. Jpn J Allergol 1994;43:679–688.
  7. Watanabe M, Watanabe J, Sonoyama K, Tanabe S: Novel method for producing hypoallergenic wheat flour by enzymatic fragmentation of the constituent allergens and its application to food processing. Biosci Biotechnol Biochem 2000;64:2663–2667.
  8. Yamada K, Urisu A, Kakami M, Koyama H, Tokuda R, Wada E, Kondo Y, Ando H, Morita Y, Torii S: IgE-binding activity to enzyme-digested ovomucoid distinguishes between patients with contact urticaria to egg with and without overt symptoms on ingestion. Allergy 2000;55:565–569.
  9. Host A, Halken S: Hypoallergenic formulas – when, to whom and how long: after more than 15 years we know the right indication! Allergy 2004;59(suppl 78):45–52.
  10. Schlichtherle-Cerny H, Amado R: Analysis of taste-active compounds in an enzymatic hydrolysate of deamidated wheat gluten. J Agric Food Chem 2002;50:1515–1522.
  11. Tanabe S, Watanabe J, Oyama K, Fukushi E, Kawabata J, Arai S, Nakajima T, Watanabe M: Isolation and characterization of a novel polysaccharide as a possible allergen occurring in wheat flour. Biosci Biotechnol Biochem 2000;64:1675–1680.
  12. 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.
  13. Tanabe S, Tesaki S, Yanagihara Y, Mita H, Takahashi K, Arai S, Watanabe M: Inhibition of basophil histamine release by a haptenic peptide mixture prepared by chymotryptic hydrolysis of wheat flour. Biochem Biophys Res Commun 1996;223:492–495.
  14. Maynard F, Jost R, Wal JM: Human IgE binding capacity of tryptic peptides from bovine alpha-lactalbumin. Int Arch Allergy Immunol 1997;113:478–488.
  15. Kurisake J, Konishi Y, Kaminogawa S, Yamuchi K: Studies on the allergenic structure of hen ovomucoid by chemical and enzymic fragmentation. Agric Biol Chem 1981;45:879.
  16. Elsayed S, Hammer AS, Kalvenes MB: Antigenic and allergenic determinants of ovalbumin. 1. Peptide mapping, cleavage at the methionyl peptide bonds and enzymic hydrolysis of native and carboxymethyl OA. Int Arch Allergy Appl Immunol 1986;79:101–107.
  17. van Beresteijn EC, Peeters RA, Kaper J: Molecular mass distribution, immunological properties and nutritive value of whey protein hydrolysates. J Food Prot 1994;57:619–625.
  18. Huby RDJ, Dearman RJ, Kimber I: Why are some proteins allergen? Toxicol Sci 2000;55:235–246.

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