Okayama Prefectural Technology Center for Agriculture, Forestry, and Fisheries, Research Institute for Biological Sciences (RIBS), 7549-1 Kibichuo-cho, Kaga-gun, Okayama, 716-1241, Japan.
Department of Food Science, College of Animal Science, Southwest University, Rongchang Campus, Rongchang, Chongqing, 402460, China.
Appl Biochem Biotechnol. 2019 Feb;187(2):570-582. doi: 10.1007/s12010-018-2839-7. Epub 2018 Jul 16.
Cow's milk is one of the most common allergenic foods. Cow's milk allergy is mainly an IgE-mediated hypersensitivity reaction, and the major allergens from cow's milk have been found to be caseins, β-lactoglobulin, and α-lactalbumin. Several peptides derived from bovine casein are known allergens in cow's milk. To reduce their allergenicity, these proteins can be degraded by food-grade peptidases. We succeeded in detection of two peptides, VLPVPQK and FFVAPFPEVFGK, from bovine casein-derived allergen peptides by using an ion trap LC-MS apparatus. This study focuses on the synergistic effects of Streptomyces aminopeptidases belonging to the M1, M24, and M28 families on the degradation of the allergen peptides. From these results, we demonstrated that the combination of M1 and M24 aminopeptidases was the most effective for degrading the abovementioned allergenic peptides.
牛奶是最常见的过敏原食物之一。牛奶过敏主要是一种 IgE 介导的过敏反应，已发现牛奶中的主要过敏原是酪蛋白、β-乳球蛋白和α-乳白蛋白。几种来自牛酪蛋白的肽被认为是牛奶中的过敏原。为了降低其致敏性，可以使用食品级肽酶对这些蛋白质进行降解。我们成功地使用离子阱 LC-MS 仪器检测到两种来自牛酪蛋白衍生过敏原肽的肽，VLPVPQK 和 FFVAPFPEVFGK。本研究重点研究了属于 M1、M24 和 M28 家族的链霉菌氨肽酶对过敏原肽降解的协同作用。根据这些结果，我们证明 M1 和 M24 氨肽酶的组合对上述过敏原肽的降解最有效。
