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In the last years, legume proteins are gaining importance as food ingredients because of their nutraceutical properties. However, legumes are also considered relevant in the development of food allergies through ingestion. Peanuts and soybeans are important food allergens in Western countries, while lentil and chickpea allergy are more relevant in the Mediterranean area. Information about the effects of thermal-processing procedures at various temperatures and conditions is scarce; therefore, the effect of these procedures on legume allergenic properties is not defined so far. The SDS-PAGE and IgE-immunoblotting patterns of chickpeas and lentils were analyzed before and after boiling (up to 60 min) and autoclaving (1.2 and 2.6 atm, up to 30 min). The results indicated that some of these treatments reduce IgE binding to lentil and chickpea, the most important being harsh autoclaving. However, several extremely resistant immunoreactive proteins still remained in these legumes even after this extreme treatment.

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Novel snack-type functional foods based on extruded lentil flours could convey the related health benefit of their bioactive compounds, provide a gluten-free alternative to consumers, and potentially increase the consumption of pulses. Extrusion treatment promoted an increase in galactopinitol, ciceritol, raffinose, stachyose and total α-galactoside content, in most lentil flours. As α-galactosides may act as prebiotics, they could convey beneficial effects to human and monogastric animals. Conversely, extrusion significantly (p < 0.05) reduced the inositol hexaphosphate content to less phosphorylated phytates (inositol pentaphosphate and inositol tetraphosphate), which provide health effects. The gluten-free formulation (control formulation #3) presented the highest significant (p < 0.05) drop in the inositol hexaphosphate of 14.7-fold decrease, but had a large increase in inositol pentaphosphate, due to extrusion processing. These two results are desirable in the finished product. Extrusion also caused a significant (p < 0.05) reduction in the trypsin content and completely inactivated lectin, in all processed samples.