Abstract：
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.
摘要：
酪蛋白,牛奶中的主要过敏原，在为过敏儿童提供营养支持方面提出了重大挑战。为了解决这个问题，我们研究了一种复合酶，包括木瓜蛋白酶和胰凝乳蛋白酶,降低酪蛋白的致敏性。酶水解诱导酪蛋白的实质性结构变化，降低其对特异性IgE和IgG抗体的亲和力。此外,在BALB/c小鼠模型中，酪蛋白水解物缓解过敏症状，较低的血清IgE和IgG水平证明，降低血浆组胺，细胞共培养过程中Th2细胞因子释放减少。肽分析显示，与木瓜蛋白酶和胰凝乳蛋白酶相比，复合酶水解的酪蛋白中含有IgE表位的肽减少了52.38％和60％，分别,以及明显缺乏先前报道的T细胞表位。这些结果证明了酶组合在变应原性蛋白中增强表位破坏效率的潜力。为低过敏性乳制品的开发提供有价值的见解。
