4.6 Review

Dairy bioactive proteins and peptides: a narrative review

Journal

NUTRITION REVIEWS
Volume 79, Issue -, Pages 36-47

Publisher

OXFORD UNIV PRESS INC
DOI: 10.1093/nutrit/nuab097

Keywords

alpha-lactalbumin; angiotensin-converting enzyme; bioactive peptides; glycomacropeptide; whey protein

Funding

  1. National Dairy Council

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Milk proteins are known for their high nutritional quality due to their essential amino acid composition and various bioactivities, and can be easily separated into casein and whey fractions. Encrypted peptides in these proteins are increasingly recognized as beneficial biologically active metabolites for human health.
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.

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