Potential allergenicity and hydrolysis assessment of bovine casein and β‐casein by treatment with lactic acid bacteria

Abstract

Casein is one of the main allergens in cow's milk, accounting for 80% of cow's milk proteins. The ability of hydrolyzing proteins by bacteria is also different. In this study, the capacity of lactic acid bacteria to hydrolyze casein or β‐casein and the IgG/IgE‐binding capacity of hydrolysates were evaluated. The intensity of casein and β‐casein degradation was analyzed by SDS–PAGE and RP–HPLC. The hydrolysates were tested for their capacity to inhibit IgG and IgE binding by ELISA. The peptides in the hydrolysate were also analyzed by LC–MS/MS. In these strains, Lactobacillus rhamnosus (CICC No. 22175) had the strongest hydrolysis of casein and β‐casein. The hydrolysate of Lactobacillus rhamnosus (CICC No. 22175) showed the lowest antigenicity and potential allergenicity. It also hydrolyzed major allergen IgE epitopes and preserved T cell epitopes. Thereore Lactobacillus rhamnosus (CICC No. 22175) could be used for developing hypoallergenic dairy products and the development of tolerance. Practical applications By the study, it obtained that a strain of Lactobacillus rhamnosus could effectively degrade casein and reduced the potential allergenicity of casein. At the same time, some major allergic epitopes were hydrolyzed and T cell epitopes were preserved. Therefore, it is very valuable for the application and development of lactic acid bacteria. The hydrolysate can also be used in a new hypoallergenic dairy formula with specific health benefits and promoting oral tolerance.

Mass Spectrometry Analysis on the Breakage of Allergens in High-Molecular-Mass Polymer of Roasted Peanuts

“…In our previous studies, we observed that allergens in roasted peanuts undergo degradation and cross-linking. , At high temperatures, this process has been found to induce breakage of proteins, which may have the potential to break antigenic epitopes . All these structural changes may potentially influence the properties of allergens …”

“…16 All these structural changes may potentially influence the properties of allergens. 17 However, limited research has been conducted on the exact breakage sites of allergens, which can provide valuable insights into the mechanisms of allergenicity and sensitization change. The breakage of allergens during processing may disrupt IgE epitopes, which are crucial for immunological recognition and response.…”

Research progress on the mechanism of probiotics regulating cow milk allergy in early childhood and its application in hypoallergenic infant formula

“…As one of the important probiotics, lactic acid bacteria can not only regulate the composition of intestinal flora to play an immunomodulatory function or produce a variety of stimulus signals to activate immune cells, thereby triggering systemic immune response ( 110 ). On the other hand, lactic acid bacteria have a complex protease system ( 111 ), which can produce peptidase and protease to hydrolyze milk protein, destroy allergen epitopes ( 112 ), and thus reduce milk allergy ( 113 ).…”

Screening of probiotic Lactobacillus to reduce peanut allergy and with potential anti‐allergic activity

“…22175 can effectively hydrolyzed casein and significantly reduced its sensitization. 15 Peanuts are primarily processed through boiling or frying in China, and through other processes such as baking in other countries, indicating that China might have fewer peanut allergy patients than other countries. 16 So, appropriate treatment may lead to the reduction of peanut allergenicity, and in Europe and the USA the number suffering from peanut allergies is very large.…”

“…Huang selected LAB to degrade casein and β ‐casein, and finally found that L. rhamnus CICC No. 22175 can effectively hydrolyzed casein and significantly reduced its sensitization 15 …”