A composite enzyme derived from papain and chymotrypsin reduces the Allergenicity of Cow's Milk allergen casein by targeting T and B cell epitopes.

Food Chem

State Key Laboratory of Food Science and Resources, Nanchang University, Nanchang, Jiangxi 330047, P. R. China; Sino-German Joint Research Institute, Nanchang University, Nanchang, Jiangxi 330047, P. R. China; Jiangxi Province Key Laboratory of Food Allergy, Nanchang University, Nanchang, Jiangxi 330047, P. R. China.

Published: November 2024

Casein, the major allergen in cow's milk, presents a significant challenge in providing nutritional support for children with allergies. To address this issue, we investigated a composite enzyme, comprising papain and chymotrypsin, to reduce the allergenicity of casein. Enzymatic hydrolysis induced substantial structural changes in casein, diminishing its affinity for specific IgE and IgG antibodies. Additionally, in a BALB/c mouse model, casein hydrolysate alleviated allergic symptoms, evidenced by lower serum IgE and IgG levels, reduced plasma histamine, and decreased Th2 cytokine release during cell co-culture. Peptidomic analysis revealed a 52.38% and 60% reduction in peptides containing IgE epitopes in casein hydrolyzed by the composite enzyme compared to papain and chymotrypsin, respectively, along with a notable absence of previously reported T cell epitopes. These results demonstrate the potential of enzyme combinations to enhance the efficiency of epitope destruction in allergenic proteins, providing valuable insights into the development of hypoallergenic dairy products.

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http://dx.doi.org/10.1016/j.foodchem.2024.140315DOI Listing

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