Profile Analysis and Immunoglobulin E Reactivity of Wheat Protein HydrolysatesAkiyama H.a · Sakata K.a · Yoshioka Y.a · Murata Y.c · Ishihara Y.d · Teshima R.b · Sawada J.b · Maitani T.a
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.
© 2006 S. Karger AG, Basel
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