Exploring the proteolytic activity of Lactiplantibacillus plantarum AHQ-14 to reduce the allergenicity of milk protein and its probiotic potential based on peptidomics and genomics

In our previous work, Lactiplantibacillus plantarum AHQ-14 was isolated from the conventional fermented dairy products in Xinjiang district (China) for its strong ability to reduce the antigenicity of bovine milk β-LG. Although its probiotic properties and safety were evaluated in vitro, it is necessary to further explore the effect of L. plantarum AHQ-14 on the major allergenic proteins and its mechanism of action and probiotic potential by peptidomics and genomics in this study. The results showed that the hydrolysis ability of L. plantarum AHQ-14 to α-LA, β-LG, and α-CN was the strongest at 10 h of incubation, and their IgE binding inhibition rates were also higher. Peptidomics results showed that L. plantarum AHQ-14 could destroy the main allergic epitopes of α-LA, β-LG, α-CN, and obtain a variety of bioactive peptides. Genomics results revealed L. plantarum AHQ-14 contained a great deal of genes encoding a phosphoenolpyruvate-dependent glucose phosphate transport system, a complete Opp oligopeptide transport system, and abundant peptidase-related genes, and indicated that L. plantarum AHQ-14 had a strong ability to metabolize and transport carbohydrates and AA, as well as strong hydrolyze proteins. Lactiplantibacillus plantarum AHQ-14 also had probiotic potential in pathogen defense and immune stimulation, and strong environmental adaptability. This study laid a foundation for the practical utilization of L. plantarum AHQ-14 and the further development of other probiotics with potential to reduce allergenicity of proteins.