Commercial soybean lecithins: a source of hidden allergens?
- Cite this article as:
- Müller, U., Weber, W., Hoffmann, A. et al. Z Lebensm Unters Forsch (1998) 207: 341. doi:10.1007/s002170050343
- 157 Downloads
Soybeans are known to be allergenic for adults as well as for infants. Processed products derived from soybeans are used in a wide spectrum of foods, drugs and other industrial products. In particular, soybean lecithins are used as stabilizers and emulsifiers and may not be suspected as possible source of allergens. To test this hypothesis, six commercial soy lecithins were investigated for residual allergenicity and compared with extracts from raw and heat-treated soybeans. They were characterized, the protein content was determined by enzyme-linked immunosorbent assay (ELISA) and allergens were analyzed with specific IgE from patients' sera using the enzyme allergosorbent test (EAST), EAST inhibition and protein blotting followed by immunodetection. For further characterization a polyclonal antiserum directed against soybean extract and a monoclonal antibody (mAb 025) directed against the acidic subunit of the soybean storage protein glycinin were used. The EAST studies revealed that three of six sera from patients with allergy to soybeans contained IgE to four soy lecithins (Topcithin 50, Topcithin 300, Emulfluid FD 12, Epikuron 100 P), the same lecithins which were found to contain residual proteins. Two lecithins with a protein content of less than 20 ppb did not bind IgE. EAST inhibition showed that the allergens from soy lecithin were immunologically more closely related to allergens from heat-treated soybeans than to those from raw soybeans. Protein blotting and immunodetection of the protein extract from the lecithins resulted in various allergen bands between 14 kDa and 94 kDa. A heat-stable allergen of 39 kDa was recognized by the monoclonal antibody and thus identified as a subunit of glycinin. The results obtained were confirmed by a mediator release assay based on a rat basophil leukemia cell line. Lecithins that contained residual proteins caused a specific mediator release, suggesting that these products may induce allergic symptoms. Our results show that soybean lecithins are capable of introducing hidden allergens to processed foods and that the IgE binding potential corresponds to the total protein determined by ELISA. Furthermore, it appears to be possible that by monitoring the protein content soy lecithins can be applied which may be safe for the allergic consumer.