Leila Ben Farhat, Hiba Selmi, Violetta Toth, Amanda Hoarau, Agnes Suli, Kata Sara Labas, Abidi Ferid, Edit Mikó
{"title":"A2 Milk: The Impact of Genetic Variation in Milk Protein on Human Health.","authors":"Leila Ben Farhat, Hiba Selmi, Violetta Toth, Amanda Hoarau, Agnes Suli, Kata Sara Labas, Abidi Ferid, Edit Mikó","doi":"10.2174/0113892037366987250401183000","DOIUrl":null,"url":null,"abstract":"<p><p>Recently, a new type of cow's milk has been commercialized in the markets, called A2 milk. It is derived from a specific allelic composition on chromosome 6. The only difference between A1 and A2 milk results from the polymorphism at the 67 amino acid chain. In this position, A2 milk has a proline amino acid, while A1 milk has a histidine amino acid. Proteins are one of the most important components of milk, especially casein, and have received significant attention as they are the source of bioactive opioid peptides called beta-casomorphin-7. Peptides are released through enzymatic digestion of casein and whey proteins. More precisely, this bioactive peptide is produced by sequential gastrointestinal digestion of bovine A1 variants proteins, while this phenomenon is not present in variant A2. Studies have reported that A1 milk can be harmful to health not only for adults but also for infants and that β-casein A2 becomes a safer choice following the relationship between disease risk and consumption of the beta-casomorphin-7 peptide. Indeed, epidemiological studies suggest that the released beta-casomorphin-7 peptide is a risk factor for the development of diseases in humans, but this has not yet been validated by other studies. In contrast, A2 milk has been suggested as an appropriate substitute for A1 milk since populations consuming milk containing high levels of the A2 beta-casein variant have lower rates of diseases, such as diabetes, coronary heart disease, autism, and schizophrenia.</p>","PeriodicalId":10859,"journal":{"name":"Current protein & peptide science","volume":" ","pages":""},"PeriodicalIF":1.9000,"publicationDate":"2025-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current protein & peptide science","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.2174/0113892037366987250401183000","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Recently, a new type of cow's milk has been commercialized in the markets, called A2 milk. It is derived from a specific allelic composition on chromosome 6. The only difference between A1 and A2 milk results from the polymorphism at the 67 amino acid chain. In this position, A2 milk has a proline amino acid, while A1 milk has a histidine amino acid. Proteins are one of the most important components of milk, especially casein, and have received significant attention as they are the source of bioactive opioid peptides called beta-casomorphin-7. Peptides are released through enzymatic digestion of casein and whey proteins. More precisely, this bioactive peptide is produced by sequential gastrointestinal digestion of bovine A1 variants proteins, while this phenomenon is not present in variant A2. Studies have reported that A1 milk can be harmful to health not only for adults but also for infants and that β-casein A2 becomes a safer choice following the relationship between disease risk and consumption of the beta-casomorphin-7 peptide. Indeed, epidemiological studies suggest that the released beta-casomorphin-7 peptide is a risk factor for the development of diseases in humans, but this has not yet been validated by other studies. In contrast, A2 milk has been suggested as an appropriate substitute for A1 milk since populations consuming milk containing high levels of the A2 beta-casein variant have lower rates of diseases, such as diabetes, coronary heart disease, autism, and schizophrenia.
期刊介绍:
Current Protein & Peptide Science publishes full-length/mini review articles on specific aspects involving proteins, peptides, and interactions between the enzymes, the binding interactions of hormones and their receptors; the properties of transcription factors and other molecules that regulate gene expression; the reactions leading to the immune response; the process of signal transduction; the structure and function of proteins involved in the cytoskeleton and molecular motors; the properties of membrane channels and transporters; and the generation and storage of metabolic energy. In addition, reviews of experimental studies of protein folding and design are given special emphasis. Manuscripts submitted to Current Protein and Peptide Science should cover a field by discussing research from the leading laboratories in a field and should pose questions for future studies. Original papers, research articles and letter articles/short communications are not considered for publication in Current Protein & Peptide Science.