Influence of minor β-CN genotypes on coagulation properties and proteolytic pathways of bovine milk
| dc.contributor.author | Gai, Nan | en |
| dc.contributor.author | Uniacke-Lowe, Therese | en |
| dc.contributor.author | Goulding, David A. | en |
| dc.contributor.author | O'Regan, Jonathan | en |
| dc.contributor.author | Affolter, Michael | en |
| dc.contributor.author | Kelly, Alan L. | en |
| dc.contributor.funder | Société des Produits Nestlé | en |
| dc.contributor.funder | Teagasc Food Research Centre | en |
| dc.date.accessioned | 2025-07-22T10:59:35Z | |
| dc.date.available | 2025-07-22T10:59:35Z | |
| dc.date.issued | 2025-07-14 | en |
| dc.description.abstract | Numerous studies have examined the effects of the two most common β-casein (β-CN) genetic variants, A1 and A2, on the physicochemical and functional properties of bovine milk. However, relatively minor variants of this protein such as B and I remain under-researched. This study collected milk with four β-CN genotypes, A1B, A2B, A1I, and A2I, across three collection occasions to investigate their functional and proteolytic properties. Milk of the B variant exhibited similar behaviour to A1 regarding rennet and acid coagulation properties, while I was similar to A2. Furthermore, the Glu121-Arg122 and Arg122-Gln123 bonds in the β-CN B variant were more sensitive to plasmin-derived proteolysis than Ser122 in other variants, leading to more peptides from cleavage at Arg122-related sites. These findings support grouping genotypes based on the amino acid (AA) at position 67, as variants sharing the same AA at this position exhibit similar processability, while also highlighting the significant impact of AA at position 122 for proteolysis in milk or dairy products. | en |
| dc.description.status | Peer reviewed | en |
| dc.description.version | Published Version | en |
| dc.format.mimetype | application/pdf | en |
| dc.identifier.articleid | 106352 | en |
| dc.identifier.citation | Gai, N., Uniacke-Lowe, T., Goulding, D. A., O'Regan, J., Affolter, M. and Kelly, A. L. (2025) 'Influence of minor β-CN genotypes on coagulation properties and proteolytic pathways of bovine milk', International Dairy Journal, 169, 106352 (8pp). https://doi.org/10.1016/j.idairyj.2025.106352 | en |
| dc.identifier.doi | 10.1016/j.idairyj.2025.106352 | en |
| dc.identifier.endpage | 8 | en |
| dc.identifier.issn | 9586946 | en |
| dc.identifier.journaltitle | International Dairy Journal | en |
| dc.identifier.startpage | 1 | en |
| dc.identifier.uri | https://hdl.handle.net/10468/17738 | |
| dc.identifier.volume | 169 | |
| dc.language.iso | en | en |
| dc.publisher | Elsevier Ltd | en |
| dc.rights | © 2025, the Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). | en |
| dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
| dc.subject | Aspartame | en |
| dc.subject | Mammals | en |
| dc.subject | Physicochemical properties | en |
| dc.subject | Proteolysis | en |
| dc.subject | Amino-acids | en |
| dc.subject | Bovine milk | en |
| dc.subject | Coagulation properties | en |
| dc.subject | Functional properties | en |
| dc.subject | Functionals | en |
| dc.subject | Genetic variants | en |
| dc.subject | Physicochemical property | en |
| dc.subject | Processability | en |
| dc.subject | Property | en |
| dc.subject | Coagulation | en |
| dc.subject | ~Food and Nutritional Sciences - Journal Articles~ | en |
| dc.title | Influence of minor β-CN genotypes on coagulation properties and proteolytic pathways of bovine milk | en |
| dc.type | Article (peer reviewed) | en |
