Dairy bioactive proteins and peptides: a narrative review
2021/10/28 by Nancy Auestad, Donald K Layman, Donald K. Layman · 140 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Nursing · #Amino acid #Biochemistry #Biological activity #Biology #Casein #Chemistry #Complete protein #In vitro #Infant Nutrition and Health #Lactoferrin #Muscle metabolism and nutrition #Peptide #Protein Hydrolysis and Bioactive Peptides #Whey protein
paper · pdf · doi:10.1093/nutrit/nuab097
published in Nutrition Reviews 79(Supplement_2), 36-47 (Oxford University Press)
openalex publication_date 2021/10/28 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30
Abstract
Milk proteins are known for their high nutritional quality, based on their essential amino acid composition, and they exhibit a wide range of bioactivities, including satiety, antimicrobial, mineral-binding, and anti-lipidemic properties. Because of their unique water solubility, milk proteins are readily separated into casein and whey fractions, which can be further fractionated into many individual proteins, including alpha-S1- and alpha-S2-caseins, beta-casein, and kappa-casein, and the whey proteins alpha-lactalbumin, lactoferrin, beta-lactoglobulin, and glycomacropeptide. Many of these proteins have unique bioactivities. Further, over the past 30 years, peptides that are encrypted in the primary amino acid sequences of proteins and released along with amino acids during digestion are increasingly recognized as biologically active protein metabolites that may have beneficial effects on human health. This review examines the current state of the science on the contribution of dairy proteins and their unique peptides and amino acids to human health.
Citations
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