Effect of temperature on immunoreactive properties of cow milk whey protein. I. a-lactalbumin

Abstract

The effect of heat induced changes on the immunoreactivity of -lactalbumin ( -la) in whey was evaluated. Whey and acidified -la solutions were heated for various times at temperatures between 60 and 100 °C. After heating, the samples were clarified and the protein content (by Bradford's method), the quantity of -la (by FPLC method) and the immune response to an anti -la probe were determined. The samples heated at 80 °C were characterized by the highest -la immunoreactivity properties. Raising temperature up to 90 °C and 100 °C caused a marked decrease in -la immunoreactivity. As was found by FPLC method in the samples heated at 60 and 65 °C, -la content changes were not statistically significant. A gradual decrease in the content of -la was observed with increased temperature and duration of heating.

The effect of transglutaminase-induced polymerization in the presence of cysteine on β-lactoglobulin antigenicity

“…The presence of IgG antibodies against b-Lg HT TG in mice, as shown in this study, reinforces the hypothesis that these samples are immunogenic, even after heat treatment followed by the TG reaction. These findings may be explained by conformational changes occurring as a result of the heat treatment and/or the subsequent polymerization with TG, which formed and/or exposed epitopes formerly present inside the molecule, increasing the immunoreactivity (Mierzejewska & Kubicka, 2006).…”

Evaluation of Immunoreactivity of Pea (Pisum sativum) Albumins in BALB/c and C57BL/6 Mice

“…The growing number of people with various food allergies, and increasingly common incidents of cross-reactivity between epitopes from different foods have generated great interest in research on food allergies. So far, we have investigated the immunomodulatory properties of different food proteins such as soy and whey preparations, fermented milk products, lipase from rapeseeds, and mare’s milk. ,− Now, growing interest in the food industry for functional ingredients and feasible bioalternatives to meat proteins has inspired us to investigate the potential of PA, rich in EAAs and less likely to induce food allergies, as dietary supplements. Also, the spontaneous non-enzymatic attachment of monosaccharaides (glycation) of pea proteins, which often occurs during storage or technological/culinary processing of peas, affects the immunoreactivity of pea proteins.…”

Milk and Meat Allergens from Bos taurus β-Lactoglobulin, α-Casein, and Bovine Serum Albumin: An In-Vivo Study of the Immune Response in Mice

“…Removal of milk from the diet would deprive children of a source of complete proteins rich in essential amino acids, branched-chain amino acids, vitamins D and E, and macronutrients such as iron and calcium [3,4]. There are certain technological processes to reduce the allergenicity of proteins, e.g., thermal denaturation and glycation [5,6]. Fermentation by proteolytic enzymes from Lactobacillus destroys milk protein epitopes and thus reduces protein allergenicity [7,8].…”