Proteolysis of lactoferrin and β-casein in complex coacervate and uncomplexed forms during in vitro infant gastrointestinal digestion
Lactoferrin is of interest for infant nutrition due to its roles in supporting gastrointestinal development. When supplemented orally, digestive exposure may reduce the availability and biofunctionality of the protein and its derived peptides. The aim of this study was to evaluate the proteolysis of...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2024-05-01
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| Series: | Journal of Functional Foods |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1756464624001439 |
| _version_ | 1827255797296398336 |
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| author | Jasper M. van der Schaaf David A. Goulding Jonathan O'Regan Michael Affolter James A. O'Mahony Alan L. Kelly |
| author_facet | Jasper M. van der Schaaf David A. Goulding Jonathan O'Regan Michael Affolter James A. O'Mahony Alan L. Kelly |
| author_sort | Jasper M. van der Schaaf |
| collection | DOAJ |
| description | Lactoferrin is of interest for infant nutrition due to its roles in supporting gastrointestinal development. When supplemented orally, digestive exposure may reduce the availability and biofunctionality of the protein and its derived peptides. The aim of this study was to evaluate the proteolysis of bovine lactoferrin and β-casein coacervates following infant in vitro digestion. Coacervation of β-casein with lactoferrin showed a protective function against peptic proteolysis, increasing the levels of intact β-casein and lactoferrin during gastric digestion, while the uncomplexed β-casein was readily proteolyzed. The coacervate was shown to protect the C-terminal of β-casein against gastric proteolysis. This resulted in altered peptide profiles in the gastric and intestinal phases, requiring additional research to ascertain potential implications for biological activity. This study demonstrates the impact of protein–protein interactions on proteolysis during digestion, which may delay proteolysis and possibly protect the bioactive properties of the proteins. |
| first_indexed | 2024-04-24T18:48:50Z |
| format | Article |
| id | doaj.art-b23ad6031ce74718bcc43f287b37faa2 |
| institution | Directory Open Access Journal |
| issn | 1756-4646 |
| language | English |
| last_indexed | 2025-03-22T01:28:43Z |
| publishDate | 2024-05-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Functional Foods |
| spelling | doaj.art-b23ad6031ce74718bcc43f287b37faa22024-05-10T04:33:42ZengElsevierJournal of Functional Foods1756-46462024-05-01116106141Proteolysis of lactoferrin and β-casein in complex coacervate and uncomplexed forms during in vitro infant gastrointestinal digestionJasper M. van der Schaaf0David A. Goulding1Jonathan O'Regan2Michael Affolter3James A. O'Mahony4Alan L. Kelly5School of Food and Nutritional Sciences, University College Cork, Cork, IrelandNestlé Development Centre Nutrition, Wyeth Nutritionals Ireland, Askeaton, Co. Limerick, IrelandNestlé Development Centre Nutrition, Wyeth Nutritionals Ireland, Askeaton, Co. Limerick, IrelandNestlé Research, Société des Produits Nestlé SA, 1000 Lausanne, SwitzerlandSchool of Food and Nutritional Sciences, University College Cork, Cork, IrelandSchool of Food and Nutritional Sciences, University College Cork, Cork, Ireland; Corresponding author.Lactoferrin is of interest for infant nutrition due to its roles in supporting gastrointestinal development. When supplemented orally, digestive exposure may reduce the availability and biofunctionality of the protein and its derived peptides. The aim of this study was to evaluate the proteolysis of bovine lactoferrin and β-casein coacervates following infant in vitro digestion. Coacervation of β-casein with lactoferrin showed a protective function against peptic proteolysis, increasing the levels of intact β-casein and lactoferrin during gastric digestion, while the uncomplexed β-casein was readily proteolyzed. The coacervate was shown to protect the C-terminal of β-casein against gastric proteolysis. This resulted in altered peptide profiles in the gastric and intestinal phases, requiring additional research to ascertain potential implications for biological activity. This study demonstrates the impact of protein–protein interactions on proteolysis during digestion, which may delay proteolysis and possibly protect the bioactive properties of the proteins.http://www.sciencedirect.com/science/article/pii/S1756464624001439DigestionComplex coacervationIn vitro digestionLactoferrinβ-caseinProteolysis |
| spellingShingle | Jasper M. van der Schaaf David A. Goulding Jonathan O'Regan Michael Affolter James A. O'Mahony Alan L. Kelly Proteolysis of lactoferrin and β-casein in complex coacervate and uncomplexed forms during in vitro infant gastrointestinal digestion Journal of Functional Foods Digestion Complex coacervation In vitro digestion Lactoferrin β-casein Proteolysis |
| title | Proteolysis of lactoferrin and β-casein in complex coacervate and uncomplexed forms during in vitro infant gastrointestinal digestion |
| title_full | Proteolysis of lactoferrin and β-casein in complex coacervate and uncomplexed forms during in vitro infant gastrointestinal digestion |
| title_fullStr | Proteolysis of lactoferrin and β-casein in complex coacervate and uncomplexed forms during in vitro infant gastrointestinal digestion |
| title_full_unstemmed | Proteolysis of lactoferrin and β-casein in complex coacervate and uncomplexed forms during in vitro infant gastrointestinal digestion |
| title_short | Proteolysis of lactoferrin and β-casein in complex coacervate and uncomplexed forms during in vitro infant gastrointestinal digestion |
| title_sort | proteolysis of lactoferrin and β casein in complex coacervate and uncomplexed forms during in vitro infant gastrointestinal digestion |
| topic | Digestion Complex coacervation In vitro digestion Lactoferrin β-casein Proteolysis |
| url | http://www.sciencedirect.com/science/article/pii/S1756464624001439 |
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