The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Applications for α-lactalbumin in human nutrition
Open accessAbstract
α-Lactalbumin is a whey protein that constitutes approximately 22% of the proteins in human milk and approximately 3.5% of those in bovine milk. Within the mammary gland, α-lactalbumin plays a central role in milk production as part of the lactose synthase complex required for lactose formation, which drives milk volume. It is an important source of bioactive peptides and essential amino acids, including tryptophan, lysine, branched-chain amino acids, and sulfur-containing amino acids, all of which are crucial for infant nutrition. α-Lactalbumin contributes to infant development, and the commercial availability of α-lactalbumin allows infant formulas to be reformulated to have a reduced protein content. Likewise, because of its physical characteristics, which include water solubility and heat stability, α-lactalbumin has the potential to be added to food products as a supplemental protein. It also has potential as a nutritional supplement to support neurological function and sleep in adults, owing to its unique tryptophan content. Other components of α-lactalbumin that may have usefulness in nutritional supplements include the branched-chain amino acid leucine, which promotes protein accretion in skeletal muscle, and bioactive peptides, which possess prebiotic and antibacterial properties. This review describes the characteristics of α-lactalbumin and examines the potential applications of α-lactalbumin for human health.
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Dairy bioactive proteins and peptides: a narrative review
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Metadata
- Authors
- Layman, D. K., Lönnerdal, B., & Fernstrom, J. D.
- Venue
- Nutrition Reviews
- Publisher
- Oxford University Press (OUP)
- Published
- 2018-03-29
- Volume
- 76
- Issue
- 6
- Pages
- 444-460
- ISSN
- 0029-6643 (ISSN-L)
- 1753-4887
- OpenAlex
- W2794548917
- Cited by
- 316
- References
- 16
- FWCI
- 7.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
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