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Peanut is a major allergenic product. Manufacturing processes used in food industries to improve the physicochemical properties of food-based peanut (stabilization, texturization), could cause a modification of the digestibility of peanut proteins and, consequently, their allergenicity. This study aimed at examining the influence of polysaccharides, i.e., gum arabic, low methylated pectin (LMP) and xylan, on the in vitro hydrolysis of peanut protein isolate (PPI) and the in vitro allergenicity of the digestion products. PPI was hydrolysed during a two-step in vitro hydrolysis by pepsin, followed by a trypsin/chymotrypsin (T/C) mixture performed in dialysis bags with molecular weight cut-offs (MWCO) of 1000 or 8000 Da. SDS-PAGE electrophoresis and immunoblotting were assessed on the peptic and T/C digestion products in (retentates) and out of the dialysis bags (dialysates). Hydrolysis by all of the digestive enzymes showed retention of some proteins in the dialysis bags in the presence of gum arabic and xylan. The retentates were recognized by IgG and IgE, particularly peptides <20 kDa. The IgE binding with peptides of retentate containing xylan from the dialysis bag with an MWCO of 1000 Da was reduced. The immunoreactivity of hydrolysis products in dialysates was considerably reduced by polysaccharides, regardless of the dialysis bag. Reduction of PPI hydrolysis was probably due to non-specific interactions between polysaccharides and peptides. In retentates, IgE-binding epitopes were reduced by digestion and the presence of xylan. In dialysates, they were reduced by all of the polysaccharides. This work highlights the possibility of modulating this food allergy through optimized formulation. [ABSTRACT FROM AUTHOR]

Background: The major allergen of Baltic cod (Gadus callarias) is a 12.3-kDa parvalbumin with two calcium-binding sites corresponding to EF-hand motifs. Our group found a 24-kDa IgE-reactive band that was also recognized by a monoclonal antiparvalbumin antibody in Atlantic cod (Gadus morhua). Our purpose was to purify and to determine the cDNA deduced sequence of this new cod allergen. Methods: Proteins from pre rigor morris Atlantic cod were separated by gel filtration and the eluted peaks were analysed by SDS-PAGE and Western blotting with sera of sensitized patients and with antiparvalbumin. Protein bands were microsequenced, RNA transcripts were amplified by reverse transcription and polymerase chain reaction (RT-PCR) using primer combinations overlapping the open reading frame. Results: Four IgE and antiparvalbumin reactive proteins (12.5, 24, 38 and 51 kDa) were detected in gel filtration eluate. The cDNA deduced sequence of the 24 kDa protein had 109 amino acid residues with a molecular weight of 11.5 kDa and a theoretical pI of 4.34. The 24 kDa band corresponded therefore to a dimer of a β-parvalbumin. Its homology was higher with Sal sI than with Gad cI. This new allergen was named Gad mI. Conclusion: We have characterized a new parvalbumin allergen in Gadus morhua. This protein formed oligomers in native and in reducing conditions. Gad mI and Gad cI may correspond to two distinct genes of Gadus species. [ABSTRACT FROM AUTHOR]