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

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 beta-casein and the IgG/IgE-binding capacity of hydrolysates were evaluated. The intensity of casein and beta-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 beta-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.

Automated summary

Lactobacillus rhamnosus was found to effectively degrade casein and reduce its potential allergenicity in this study. It hydrolyzed major allergen epitopes while preserving T cell epitopes. This is valuable for the application and development of lactic acid bacteria, and the hydrolysate can be used in hypoallergenic dairy products with specific health benefits and promoting oral tolerance.