Efficient reduction of β-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816
Milk allergy is one of the most common food allergies, affecting 6 % of young children, and β-lactoglobulin (β-LG) is the main milk allergen. Clostridium tyrobutyricum Z816 was selected for the degradation of β-LG, which was successfully reduced by about 90 % using permeabilized bacteria under the o...
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| Format: | Article |
| Language: | English |
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Tsinghua University Press
2023-05-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S221345302200204X |
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| author | Qianru Zhao Yuwei Wang Zhengming Zhu Quanyu Zhao Liying Zhu Ling Jiang |
| author_facet | Qianru Zhao Yuwei Wang Zhengming Zhu Quanyu Zhao Liying Zhu Ling Jiang |
| author_sort | Qianru Zhao |
| collection | DOAJ |
| description | Milk allergy is one of the most common food allergies, affecting 6 % of young children, and β-lactoglobulin (β-LG) is the main milk allergen. Clostridium tyrobutyricum Z816 was selected for the degradation of β-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 β-LG. Finally, the concentration and digestibility of β-LG in actual samples was quantified using enzyme-linked immunosorbent assay (ELISA) and gastrointestinal digestion simulation experiments. The results showed more than 92 % of β-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 β-LG and reduce the occurrence of milk allergies, which has great significance for the development of hypoallergenic dairy products. |
| format | Article |
| id | doaj-art-41f7eb388bd541e58c728b74dbbe2bfb |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2023-05-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-41f7eb388bd541e58c728b74dbbe2bfb2025-02-03T05:15:35ZengTsinghua University PressFood Science and Human Wellness2213-45302023-05-01123809816Efficient reduction of β-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816Qianru Zhao0Yuwei Wang1Zhengming Zhu2Quanyu Zhao3Liying Zhu4Ling Jiang5College of Biotechnology and Pharmaceutical Engineering, State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing 210009, China; College of Food Science and Light Industry, Nanjing Tech University, Nanjing 210009, ChinaCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 210009, ChinaCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 210009, ChinaSchool of Pharmaceutical Sciences, Nanjing Tech University, Nanjing 211816, ChinaSchool of Chemistry and Molecular Engineering, Nanjing Tech University, Nanjing 210009, China; Corresponding authors.College of Food Science and Light Industry, Nanjing Tech University, Nanjing 210009, China; Corresponding authors.Milk allergy is one of the most common food allergies, affecting 6 % of young children, and β-lactoglobulin (β-LG) is the main milk allergen. Clostridium tyrobutyricum Z816 was selected for the degradation of β-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 β-LG. Finally, the concentration and digestibility of β-LG in actual samples was quantified using enzyme-linked immunosorbent assay (ELISA) and gastrointestinal digestion simulation experiments. The results showed more than 92 % of β-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 β-LG and reduce the occurrence of milk allergies, which has great significance for the development of hypoallergenic dairy products.http://www.sciencedirect.com/science/article/pii/S221345302200204XMilk allergyβ-LactoglobulinClostridium tyrobutyricumPermeabilized bacteria |
| spellingShingle | Qianru Zhao Yuwei Wang Zhengming Zhu Quanyu Zhao Liying Zhu Ling Jiang Efficient reduction of β-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816 Food Science and Human Wellness Milk allergy β-Lactoglobulin Clostridium tyrobutyricum Permeabilized bacteria |
| title | Efficient reduction of β-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816 |
| title_full | Efficient reduction of β-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816 |
| title_fullStr | Efficient reduction of β-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816 |
| title_full_unstemmed | Efficient reduction of β-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816 |
| title_short | Efficient reduction of β-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816 |
| title_sort | efficient reduction of β lactoglobulin allergenicity in milk using clostridium tyrobutyricum z816 |
| topic | Milk allergy β-Lactoglobulin Clostridium tyrobutyricum Permeabilized bacteria |
| url | http://www.sciencedirect.com/science/article/pii/S221345302200204X |
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