In this study, the in vivo allergenicity of bovine beta-lactoglobulin (BLG) in peptic whey protein hydrolysates generated during microwave and conventional heating treatments was assessed. The allergenicity of the hydrolysates was explored by studying the reaction of the murine jejunum from previously immunised Balb/c mice to treated BLG in an Ussing chamber. Intestinal anaphylactic reactions after stimulation of the gut-associated immune system are a good indicator of potential in vivo allergenicity of whey hydrolysates. Fifty-two per cent of BLG was hydrolysed by pepsin after only 3 min of microwave irradiation at 200 watts (W), yet it remained intact under conventional heating. Far-and near-UV circular dichroism spectra indicated significant changes in BLG secondary and tertiary structures with microwave irradiation at 200 W. Pepsin whey protein hydrolysates obtained with microwave irradiation at 200 W for 3 min did not stimulate secretion of chloride in the Ussing chamber, as shown by the intensity of the short current values recorded (27.86 lA cm À2 ), compared to the conventional pepsin hydrolysates (68.21 lA cm À2 ). This demonstrates the low allergenicity of whey protein hydrolysates generated in this manner. These results confirm that microwave treatment combined with peptic hydrolysis could be applied to produce low allergenicity milk peptides.
In our study, we tried to investigate the allergenic properties of bovine lactoferrin (bLf) at different doses. The lactoferrin (LF) allergenicity was explored using murine model of allergy through measuring anti-LF IgG, IgG1 and IgE antibodies (Abs) responses and by in vivo anaphylactic reactions in LF sensitized mice. A histological examination of intestinal lamina propria was performed to assess gut inflammation. Four groups of mice (Balb/ c) were sensitized intraperitoneally to bLf using different doses (1%, 2%, 5% and 10%). Histological study of intestinal lamina propria revealed a marked decrease in villus length in 5% and 10% sensitized mice groups. Also, high levels of anti-bLf IgG and IgE were observed. Concerning the in vivo reactions, all groups developed clinical symptoms of anaphylactic reactions at different stages. Our findings show that LF-sensitized mice at 5% and 10% developed important clinical symptoms after intraperitoneal challenge with LF.
Problem statement: Cow's Milk Allergy (CMA) is a common disease in childhood. Pathophysiological mechanisms involved in gastrointestinal symptoms are relatively poorly understood. Approach: Therefore, an experimental model of intestinal anaphylaxis was needed to approach the problem. The aim of this study was to examine the effect of the parenteral sensitization to whey proteins through immune response and local intestine inflammation using a murine model of allergy. Sensitization of Balb/c mice with β-lactoglobulin (β-Lg) or whey was performed in presence of Alum Al (OH3). Mice were analyzed for β-Lg or whey specific serum antibodies by ELISA. Local anaphylactic responses were performed in vitro in using chamber by intestine challenge with β-Lg or whey. Histological study was used to assess gut inflammation. Results: The sensitization induced the production of anti-β-Lg or anti whey IgG, IgG1, IgG2a and IgE with a high IgG1/IgG2a ratio translating Th2 type response. The addition of β-Lg or whey to the serosal side of the mouse intestinal epithelium in using chamber produced electrogenic chloride secretion as shown by Isc stimulation. Histological findings were mild with villi atrophy and lymphocyte hyperplasia. Conclusion: After sensitization, the mice became prone to developing anaphylactic response and may be useful experimental model for mechanistic studies of CMA or for hydrolyzed formulae.
Problem statement: Our aim was to enhance the data on antigenic properties of dromedary whey proteins. Approach: The identification of the whey proteins was carried by SDS-page and Reversed phase high performance liquid chromatography (RP-HPLC). The cross-reactivity of dromedary whey proteins with IgG anti bovine β-lactoglobulin and anti bovine α-lactalbumin, obtained by immunisation of Balb/c mice, was carried out by ELISA. Results: The SDS-page showed the presence of band corresponding to α-lactalbumin and albumin serum; this was confirmed by the chromatogram obtained by RP-HPLC, where we detected a pick corresponding to α-lactalbumin. There was a cross reaction of dromedary whey proteins with IgG anti bovin α- lactalbumin but it was very weak with IgG anti boin β-lactoglobulin. Conclusion: We detected a cross reactivity between dromedary whey proteins and IgG anti bovin α-lactalbumin.
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