Modification of IgE Binding to β-Lactoglobulin by Fermentation and Proteolysis of Cow's Milk

Abstract

The effect of fermentation by Lactobacilli and of proteolytic hydrolysis of whole milk on the IgE binding ability of beta-lactoglobulin was studied using an ELISA inhibition assay. Sera from nine adult milk allergic patients were tested. The individual sera showed a similar inhibition pattern in the changes during fermentation and proteolysis. The degradation of beta-lactoglobulin was studied with liquid chromatography. In general, fermentation with Lactobacilli gave little effect on IgE binding, even though chromatography data showed a gradual degradation of beta-lactoglobulin. Proteolysis with trypsin, however, gave extensive degradation of beta-lactoglobulin and strongly decreased IgE binding. In addition, we measured the inhibition pattern of beta-lactoglobulin in various selected commercially available fermented milk products. These showed an IgE binding capacity similar to that of nonfermented high pasteurized milk.

Effects of food processing on food allergens

“…Milk allergies are outgrown by many but not all infants [36]. Ehn et al [37] showed that Lactobacilli fermentation of milk caused proteolysis of b-lactoglobulin, one of the whey proteins known to be an allergen, but did not decrease the IgE binding when compared with its counterpart from nonfermented pasteurized milk. Trypsin hydrolysis of b-lactoglobulin, however, seemed to significantly decrease IgE binding.…”

Changes in peptic digestibility of bovine β-lactoglobulin as a result of food processing studied by capillary electrophoresis and immunochemical methods

“…Increased proteolytic degradation was observed upon heat treatment [19][20][21], in contrast to the pronounced reduction of immunoreactivity of the partially hydrolysed allergens [18]. Controversial results can be found in literature in this context.…”

Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine β-lactoglobulin

“…In spite of this, its industrial application can be limited due to its high allergenicity; this protein being, together with caseins, one of the major allergens described in bovine milk (Wal, 2001). Thus, with the purpose of increasing its degree of applicability in the food industry, the reduction of its allergenicity has been tested over recent years by use of different methods such as chemical modification of the protein (Chobert, Briand, Grinberg, & Haertlé, 1995), proteolysis (Asselin, Hébert, & Amiot, 2006;Ehn, Allmere, Telemo, Bengtsson, & Ekstrand, 2005), and physical treatments such as heating (Guo, Fox, Flynn, & Kindstedt, 1995;Iametti et al, 2002) or high pressure (Chicón, Belloque, Alonso, & López-Fandiño, 2008;Peñas, Préstamo, Baeza, Martínez-Molero, & Gómez, 2006;Stapelfeldt, Petersen, Kristiansen, Qvist, & Skibsted, 1996).…”