Wheat, allergenic proteins

Simonato, B., Pasini, G., Giannattasio, M., Peruffo, A.D., De Lazzari, F., and Curioni, A. 2001. Food allergy to wheat products The effect of bread baking and in vitro digestion on wheat allergenic proteins. A study with bread dough, crumb, and crust. JAgric Food Chem 49(11) 5668-5673. 

Other applications involve detection of adulteration of dairy products with soy, pea, and wheat proteins (Haasnoot et al., 2001), presence of asrcasein in milk (the detection threshold for this protein was 0.87pg/mL) (Muller-Renaud et al., 2005), [3-casein in milk and cheese (Muller-Renard et al., 2004), and detection of peanut allergenic proteins (the detection threshold for this protein was 0.7 pg/mL) (Mohammed et al., 2001). 

Allergenic Proteins in Wheat and Cereal The Biochemical, Biological,... 

ALLERGENIC PROTEINS IN WHEAT AND CEREAL THE BIOCHEMICAL, BIOLOGICAL, AND IMMUNOLOGICAL PROPERTIES OF MAIN CEREAL ALLERGENS... 

Application of genetic modifications in order to decrease allergenicity of food products may be very limited. In case of multigenic protein families, (e.g., wheat) complete elimination is impossible, only partial decrease in immunoreactivity can be achieved. Also, no studies have determined the long-term stability of introduced genes, whose mutation may cause serious clinical consequences in allergic people consuming modified food products that they think is harmless to them. 

Pequet, C., Lauriere, M. 2003. New allergens in hydrolysates of wheat proteins. Rev FrAlergol Immunol Clin 43 21-23. 

Cereal prolamins, named glutenins and gliadins in wheat, secalins in rye, and horde-ins in barley, are major storage proteins of the cereal grain endosperm. These sulfur-rich proteins comprise an N-terminal domain of proline- and glutamin-rich repeats and a C-terminal domain responsible for intrachain disulfide bonds (Breiteneder and Radauer 2004). So far, y-3 hordein (Hor v 21) from barley, Sec c 20 from rye, as well as Tri a 19 and Tri a 26 from wheat are included in the IUIS allergen list. 

Thioredoxins are small ubiquitous enzymes present in many species from Archaebacteria to man. They serve as general protein disulfide oxido-reductases interacting with a broad range of proteins. Allergenic thioredoxins have been identified in fungi as well as in plants. The thioredoxins from wheat (Tri a 25) and maize (Zea m 25) are related to baker s asthma, an occupational disease affecting 4%-10% of bakery workers in European countries (Holmgren 1995). 

---