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J.Leszczyńska, U.Pytasz, J.Lukamowicz, A.Lewiński
Institute of Nutritional Chemistry Principles, Technical University of Łódź
Clinic of Endocrinology, Polish Mother's Memorial Hospital - Research Institute, Łódź
Department of Laboratory Diagnostics, Polish Mother's Memorial Hospital - Research Institute, Łódź
An implementation of elimination diet is at the base of treatment of alimentary allergy. A replacement of detrimental food from patient's diet by other components of equal nutritive value is fairly possible, if the elimination concerns one or a few kinds of food only. However, the list of products, inducing positive immunological response, is often rather long, making it especially difficult when it includes products, which are common components of daily diet, as milk, wheat flower, potatoes, etc., and the nutrition concerns children in their intensive psychosomatic development. In these, so difficult cases, a modification of the allergizing component may be an alternative, leading to either reduction or elimination of immunoreactivity. Hydrolysis is the most frequent method, leading to allergenicity, used, among others, in the production of milk-substitute products, used in bottle-feeding of infants in whom, IgE presence is confirmed in their umbilical blood. In groups of infants with enhanced risk of alimentary allergy development, a delayed implementation of strongly allergizing foods - sometimes, inducting alimentary intolerance, like gluten - is recommended.
The goal of this study was an assessment of the possibilities to reduce gliadin immunoreactivity via hydrolysis, catalysed by proteolytic enzymes.
Methods. Pepsin, tripsin, chymotrtypsin, elastase, collagenase, and other agents were used in the hydrolysis reaction. The effects of performed hydrolysis were studied for different concentrations of the above mentioned enzymes, as well as with regards to time variations of the performed reactions. Gliadin immunoreactivity was determined by ELISA method of "sandwich" type, employing poly- and monoclonal antibodies.
Results. Inexplicit effects of enzymatic proteolysis on gliadin immunoreactivity were observed, in many cases, hydrolysis enhance its immunoreactivity. Further studies will be conducted, employing trials with antigliadin antibody-containing sera.
EFFECTS ON CELIAC ACTIVITY OF GLUTEN PROTEINS MODIFIED BY CHEMICAL DEAMIDATION DISTAM
Nutrition Unit University of Milan, Italy
Gluten (gliadins and glutenins) is the main source of the viscoelastic properties in a dough and exhibits functional properties. Gliadin contains the toxic factor for coeliac patients. Amino acid composition of gliadins shows figure for glutamine of about 36%. Moreover, the sequences –Pro-Ser-Gln-Gln- and –Gln-Gln-Gln-Pro- were showed to trigger the mucosal damage in celiac disease.
This investigation focused on the chemical deamidation of gluten proteins in order to modify the sequences with celiac activity with respect to the possibility to its use as functional ingredient in gluten-free food.
A 5% gluten suspension in acetic acid was heated at different conditions of time and temperature. Under such acid treatments, loss of amide groups was observed without extensive peptide bond cleavage of the gluten proteins. A different celiac activity was evidenced by studies on immunoreactivity of serum anti-gliadins IgA antibodies to modify proteins and cytotoxic effects on LoVo human adenocarcinoma cell line.
The inherent physical properties of gluten proteins (gliadins and glutenins) are uniquely suited to their use in baking and pasta production while their functional properties such as solubility, fat emulsification, gelation, foaming allow flour and isolated gluten to be used as functional ingredient in food systems. In particular, many investigators have reported that the functional properties of gluten were greatly improved by mild acid treatment.
Gliadins of wheat, hordeins of barley and secalins of rye are responsible for triggering mucosal damage in celiac disease. Amino acid composition of the toxic prolamins (alcohol-soluble proteins) shows figure for glutamine of about 36%. In particular, gliadin was shown to be the most toxic factor. Moreover, the sequences –Pro-Ser-Gln-Gln- and –Gln-Gln-Gln-Pro- were demonstrated to be common for toxic gliadin peptides in most of the in vivo and in vitro studie.
This investigation focused on the chemical deamidation of gluten proteins for the conversion of gamma-amide glutamine residues to glutamic acid residues with the concomitant release of ammonia, in order to modify the sequences with celiac activity with respect to the possibility to its use as functional ingredient in gluten-free food.
INFLUENCE OF TECHNOLOGICAL AND BIOTECHNOLOGICAL PROCESSES ON THE IMMUNOREACTIVITY OF COW MILK PROTEINS
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