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M. Carbonaro*, S. Iametti°
*Istituto Nazionale di Ricerca per gli Alimenti e la Nutrizione, Via Ardeatina, 546, 00178 Rome, Italy
°Dipartimento di Scienze Molecolari Agroalimentari, Università degli Studi di Milano, Via Celoria 2, I-20133 Milan, Italy
Absorption of food allergens, especially proteins, from the gastrointestinal tract is a key event in the induction of the allergenic response and enzymatic hydrolysis of food proteins represents a common tool for reducing the allergic reaction in sensitive consumers. Although many protein allergens retain their allergenicity after passing through the digestive tract, the relationship between protein digestibility and allergenicity is still largely unclear.
A rapid and simple in vivo digestion method with rats for the study of nutrient (protein, mineral and trace element) bioavailability in the small intestine was previously set up (Carbonaro et al., 2000). The method provides a measure of extent of protein (or other nutrient) absorption specifically in the small intestine and allows to identify interaction of protein with other food components in the gastrointestinal tract and with the gut wall. The rat model was tested with plant and animal food, included milk and milk proteins and appeared to be promising as a novel tool in studying protein allergenicity.
A different set of in vitro studies was aimed at finding conditions where proteases added to a protein solution may selectively hydrolyze only those regions of the proteins that are relevant to allergenicity, and are buried in the native protein. Some of these regions are transiently exposed in the course of physical denaturation of beta-lactoglobulin (BLG, one of the major milk allergens). Trypsin and chymotrypsin were found to be almost inactive on the folded, native forms of BLG, but both were able to hydrolyze the BLG conformers produced under sub-denaturing thermal treatment. Recognition by monoclonal antibodies indicated that the residual intact protein was the only recognizable species. None of the proteolytic fragments was immunoreactive in these tests, suggesting that these findings may represent a suitable approach to production of high-tolerance foods (Iametti et al., 2002).
Work supported by the project “TOLLELAT” from the Italian Ministry of Agricultural and Forestry Policies. This is publication n. 3 of this project.
Carbonaro M., Grant G., Cappelloni M., Pusztai A., 2000. Perspectives into factors limiting in vivo digestion of legume proteins: antinutritional compounds or storage proteins? J. Agric. Food Chem. 48, 742-749.
Iametti S., Rasmussen P., Frøkiær H., Ferranti P., Addeo F., Bonomi F., 2002. Limited proteolysis of bovine beta-lactoglobulin during thermal treatment in sub-denaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. Eur. J. Biochem. 269, 1362-1372.
CHENOPODIUM QUINOA MAY REPRESENT A VIABLE ALTERNATIVE FOR GLUTEN – FREE PRODUCTS
C. Berti, S. Iametti, M. Porrioni, F. Bonomi
Nutrition Unit University of Milan, Italy
A good deal of interest has developed as for understanding the technological and nutritive properties of minor cereals and pseudocereals - such as buckwheat, amaranth, and quinoa - as possible wheat replacement, since these grains are non toxic to people suffering from celiac disease, a genetic and permanent intolerance to prolamins of wheat, barley, and rye.
Quinoa (Chenopodium quinoa Willd) is the focus of the present work.
First, we studied some chemical and biochemical properties of quinoa proteins useful to evaluate the processing procedures most suited to transformation of quinoa into formulations apt to replace some of the traditional cereal-based products.
Then, since quinoa has not been thoroughly tested for celiac activity, the extent of recognition of quinoa flour proteins by anti-gliadin polyclonal was evaluated by using immunochemical methods. According to the methods used here, quinoa appeared to be immunochemically safe.
Quinoa (Chenopodium quinoa Willd) is an indigenous crop grown in the Andean region of Latin America. Its grain is nutritionally interesting because of the content of high-quality lysine-rich proteins, of polyunsaturated fatty acids, of micronutrients, and of vitamins C and E. This means that supplementation of cereal grains with quinoa can enhance the nutritional value of the resultant product. Also, the technological performance of quinoa flour is quite good. However, very few reports dealt with the inherent properties of quinoa flour. In particular, there is a lack of information as for the biochemical properties of quinoa proteins, which are relevant to assess their behaviour during food processing.
The use of quinoa as a food ingredient may be very interesting because this crop is very distantly related to cereals that are toxic for celiacs (Graminaceae). Celiac individuals have to adhere lifelong to a gluten-free diet, since even small amounts of gluten can result in mucosal damage. In this frame, there is not a univocal opinion about the safety of this pseudo cereal for the production of gluten-free products aimed at the nutritional needs of gluten-sensitive individuals.
The present investigation focuses on the study of those chemical and biochemical properties useful to evaluate the processing procedures most suited to transformation of quinoa into formulations apt to replace some of the traditional cereal-based products. Furthemore, in order to exploit the use of quinoa as an ingredient for gluten-free production, the extent of recognition of quinoa flour proteins by immunochemical approches was investigated.
PRODUCTION OF HYPOALLERGENIC FOOD
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