This study focuses on the effect of heating and Maillard reaction (MR) on the in vitro digestibility and rabbit IgG- and human IgE-binding properties of ovalbumin (OVA) and ovomucoid (OM) to estimate the impact of processing on their allergenicity. With the human sera studied, heat treatment significantly reduced IgE binding to both OVA and OM, whereas MR reduced the IgE binding to OVA but increased IgE binding to OM. In contrast, heat treatment significantly favored OVA digestibility but glycation impaired it, and these treatments did not affect the digestibility of OM. The changes observed in the digestibility affected the immunogenicity of the digests accordingly, so that the higher the digestibility, the lower the antibody binding. Heat treatment and glycation by MR showed an influence on the potential allergenicity of the main egg white proteins that could be related to their resistance to denaturation and digestive enzymes.

The use of soyabean proteins as meat extenders has spread significantly due to the interesting nutritional and functional properties that are present in soyabean proteins. Together with these, health and economical reasons are the major causes for the addition of soyabean proteins to meat products. Nevertheless, despite the good properties associated to soyabean proteins, there are many countries in which the addition of these proteins is forbidden or in which the addition of soyabean proteins is allowed up to a certain extent. Thus, the need of analytical methods enabling the detection of added soyabean proteins in meat products is obvious. Microscopic, electrophoretic, immunologic, and chromatographic methods are the most widely used for this purpose. However, the detection of soyabean proteins in meat products presents difficulties related to the composition (meat species, meat quality, soyabean protein source, presence of other non-meat proteins, etc.) and the processing of the meat products, and, although these analytical methods have tried to overcome all these difficulties, there is still not a method enabling quantitative assessment of soyabean proteins in all kinds of meat products.

a b s t r a c tImmunoreactivity of bovine b-lactoglobulin (b-Lg) hydrolysates obtained after a simulated gastrointestinal digestion and previously glycated via Maillard reaction with galactose, tagatose, and dextran of 10 or 20 kDa has been determined, with a view to study the effect of glycation and aggregation degree of b-Lg on its residual immunoreactivity. High levels of glycation impaired b-Lg proteolysis and, consequently, increased the IgG-and IgE-reactivities of hydrolysates, regardless of the carbohydrate used.Protein aggregation during the advanced stages of Maillard reaction had a masking effect on b-Lg epitopes, counteracting the negative effect of the lower digestibility of glycated protein on its allergenicity. Finally, the use of polysaccharides as glycation agents did not contribute to enhancement of the masking effect of the attached carbohydrate on b-Lg epitopes. These findings stress the importance of evaluating the impact of glycation on protein gastrointestinal digestibility prior to investigation of the immunoreactivity of protein Maillard complexes.

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