Identification of A1/A2 β-Casein Genotypes and Comparison of Their Digestive Properties
A1 β-casein and A2 β-casein produce different substances after digestion due to differences in primary structure. To more comprehensively explore the possible biological activity effects on the human body, by analyzing and monitoring the changes of this protein during the digestion process, the expl...
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The editorial department of Science and Technology of Food Industry
2025-03-01
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| Series: | Shipin gongye ke-ji |
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| Online Access: | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2024040342 |
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| author | Shihang LI Hongtao XU Xiao LI Meiling SUN Xinyan YANG Pengyu XIANG Zhihao YANG Chaoxin MAN Yujun JIANG |
| author_facet | Shihang LI Hongtao XU Xiao LI Meiling SUN Xinyan YANG Pengyu XIANG Zhihao YANG Chaoxin MAN Yujun JIANG |
| author_sort | Shihang LI |
| collection | DOAJ |
| description | A1 β-casein and A2 β-casein produce different substances after digestion due to differences in primary structure. To more comprehensively explore the possible biological activity effects on the human body, by analyzing and monitoring the changes of this protein during the digestion process, the exploration of the biological functions of A1/A2 β-casein is further achieved. In this study, allele-specific PCR was initially performed on milk samples collected from different cows in the pasture to identify A1 and A2 milk types. Afterwards, β-casein isolated from A1 and A2 milk was purified and characterized with the help of anion exchange chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis. Finally, a static in vitro digestion model was constructed to compare A1 and A2 β-casein in terms of digestive properties. The results showed that the concentrations of isolated and purified A1 and A2 β-casein were 0.62 mg/mL and 0.66 mg/mL and the purities were 95.28% and 96.60%. After 5.0 h of static in vitro simulated digestion, the final digestibility of both β-caseins was around 90%, and the difference was not significant. A2 β-casein exhibited a higher degree of hydrolysis of 25.34% from the beginning of the intestinal digestion phase until the end of digestion. With the increase of gastrointestinal digestion time, the particle size of the two β-caseins decreased and the absolute value of the potential increased, and the degree of change in particle size and potential was greater for A2 β-casein than for A1 β-casein. In conclusion, the present study revealed the differences in the physicochemical properties of A1 and A2 β-caseins during static in vitro digestion and indicated to some extent that A2 β-caseins might have better digestive properties than A1 β-caseins, which provided a certain scientific basis for further expanding the application of A2 β-caseins in dairy products. |
| format | Article |
| id | doaj-art-a5a62e82edda406cab16bcf0c199585e |
| institution | OA Journals |
| issn | 1002-0306 |
| language | zho |
| publishDate | 2025-03-01 |
| publisher | The editorial department of Science and Technology of Food Industry |
| record_format | Article |
| series | Shipin gongye ke-ji |
| spelling | doaj-art-a5a62e82edda406cab16bcf0c199585e2025-08-20T02:14:31ZzhoThe editorial department of Science and Technology of Food IndustryShipin gongye ke-ji1002-03062025-03-0146516016710.13386/j.issn1002-0306.20240403422024040342-5Identification of A1/A2 β-Casein Genotypes and Comparison of Their Digestive PropertiesShihang LI0Hongtao XU1Xiao LI2Meiling SUN3Xinyan YANG4Pengyu XIANG5Zhihao YANG6Chaoxin MAN7Yujun JIANG8Key Lab of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, ChinaHangzhou Chaomu Electronic Commerce Company Limited, Hangzhou 311000, ChinaKey Lab of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, ChinaHangzhou Chaomu Electronic Commerce Company Limited, Hangzhou 311000, ChinaKey Lab of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, ChinaHangzhou Chaomu Electronic Commerce Company Limited, Hangzhou 311000, ChinaHangzhou Chaomu Electronic Commerce Company Limited, Hangzhou 311000, ChinaKey Lab of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, ChinaKey Lab of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, ChinaA1 β-casein and A2 β-casein produce different substances after digestion due to differences in primary structure. To more comprehensively explore the possible biological activity effects on the human body, by analyzing and monitoring the changes of this protein during the digestion process, the exploration of the biological functions of A1/A2 β-casein is further achieved. In this study, allele-specific PCR was initially performed on milk samples collected from different cows in the pasture to identify A1 and A2 milk types. Afterwards, β-casein isolated from A1 and A2 milk was purified and characterized with the help of anion exchange chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis. Finally, a static in vitro digestion model was constructed to compare A1 and A2 β-casein in terms of digestive properties. The results showed that the concentrations of isolated and purified A1 and A2 β-casein were 0.62 mg/mL and 0.66 mg/mL and the purities were 95.28% and 96.60%. After 5.0 h of static in vitro simulated digestion, the final digestibility of both β-caseins was around 90%, and the difference was not significant. A2 β-casein exhibited a higher degree of hydrolysis of 25.34% from the beginning of the intestinal digestion phase until the end of digestion. With the increase of gastrointestinal digestion time, the particle size of the two β-caseins decreased and the absolute value of the potential increased, and the degree of change in particle size and potential was greater for A2 β-casein than for A1 β-casein. In conclusion, the present study revealed the differences in the physicochemical properties of A1 and A2 β-caseins during static in vitro digestion and indicated to some extent that A2 β-caseins might have better digestive properties than A1 β-caseins, which provided a certain scientific basis for further expanding the application of A2 β-caseins in dairy products.http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2024040342a1 β-caseina2 β-caseinallele-specific pcrin vitro mock digestiondigestive properties |
| spellingShingle | Shihang LI Hongtao XU Xiao LI Meiling SUN Xinyan YANG Pengyu XIANG Zhihao YANG Chaoxin MAN Yujun JIANG Identification of A1/A2 β-Casein Genotypes and Comparison of Their Digestive Properties Shipin gongye ke-ji a1 β-casein a2 β-casein allele-specific pcr in vitro mock digestion digestive properties |
| title | Identification of A1/A2 β-Casein Genotypes and Comparison of Their Digestive Properties |
| title_full | Identification of A1/A2 β-Casein Genotypes and Comparison of Their Digestive Properties |
| title_fullStr | Identification of A1/A2 β-Casein Genotypes and Comparison of Their Digestive Properties |
| title_full_unstemmed | Identification of A1/A2 β-Casein Genotypes and Comparison of Their Digestive Properties |
| title_short | Identification of A1/A2 β-Casein Genotypes and Comparison of Their Digestive Properties |
| title_sort | identification of a1 a2 β casein genotypes and comparison of their digestive properties |
| topic | a1 β-casein a2 β-casein allele-specific pcr in vitro mock digestion digestive properties |
| url | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2024040342 |
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