Efficient reduction of fl-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816

Milk allergy is one of the most common food allergies, affecting 6% of young children, and fl-lactoglobulin (fl-LG) is the main milk allergen. Clostridium tyrobutyricum Z816 was selected for the degradation of fl-LG, which was successfully reduced by about 90% using permeabilized bacteria under the optimized conditions. The hydrolyzed peptides were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS) and analyzed by molecular modeling, which indicated that C. tyrobutyricum Z816 could effectively degrade the antigenic epitopes of fl-LG. Finally, the concentration and digestibility of fl-LG in actual samples was quantified using enzyme-linked immunosorbent assay (ELISA) and gastrointestinal digestion simulation experiments. The results showed more than 92% of fl-LG in actual samples was hydrolyzed, and the gastric and total digestibility of whey protein isolate (WPI) was improved by 85.96% and 64.51%, respectively. Therefore, C. tyrobutyricum Z816 offers an effective method to degrade fl-LG and reduce the occurrence of milk allergies, which has great significance for the development of hypoallergenic dairy products. (c) 2023 Beijing Academy of Food Sciences. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Automated summary

In this study, Clostridium tyrobutyricum Z816 was selected to degrade fl-lactoglobulin (fl-LG). The results showed that C. tyrobutyricum Z816 could effectively degrade the antigenic epitopes of fl-LG, and over 92% of fl-LG in actual samples was hydrolyzed.