Cited by 97Protein Hydrolysis and Bioactive PeptidesProteins in Food SystemsAnimal Diversity and Health Studies

Bioactive peptides from milk: Animal determinants and their implications in human health

Open access
Vargas-Bello-Pérez, Einar, Márquez-Hernández, Roberto I., Hernández-Castellano, Lorenzo E.·2019·Journal of Dairy Research

Abstract

Milk is an important protein source in human diets, providing around 32 g protein/l (for bovine milk, which constitutes some 85% of global consumption). The most abundant milk proteins are α-lactalbumin, β-lactoglobulin, αs-casein, β-casein, and κ-casein. Besides their nutritional value, milk proteins play a crucial role in the processing properties of milk, such as solubility, water bonding, heat stability, renneting and foaming, among others. In addition, and most importantly for this review, these proteins are the main source of bioactive components in milk. Due to the wide range of proposed beneficial effects on human health, milk proteins are considered as potential ingredients for the production of health-promoting functional foods. However, most of the evidence for bioactive effects comes from in vitro studies, and there is a need for further research to fully evaluate the true potential of milk-derived bioactive factors. Animal genetics and animal nutrition play an important role in the relative proportions of milk proteins and could be used to manipulate the concentration of specific bioactive peptides in milk from ruminants. Unfortunately, only a few studies in the literature have focused on changes in milk bioactive peptides associated to animal genetics and animal nutrition. The knowledge described in the present review may set the basis for further research and for the development of new dairy products with healthy and beneficial properties for humans.

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Registry

Crossref · 10.1017/s0022029919000384

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  • Biological activity like antioxidant and ACE-inhibitory activity increases as proteolysis proceeds but only to a certain extent.

    “Biological activity like antioxidant and ACE-inhibitory activity increases as proteolysis proceeds but only to a certain extent.”

    From Antioxidant and antihypertensive activity of Gouda cheese at different stages of ripening (2022) · cites this paper as Vargas-Bello-Pérez et al., 2019

    The Abstract identifies antioxidant milk peptides, and the Cardiovascular diseases section describes ACE-inhibitory milk peptides. The Other factors influencing milk protein composition section reports increased production of peptides with ACE-inhibitory properties when an adjunct culture is used. None of these passages says that antioxidant or ACE-inhibitory activity rises as proteolysis proceeds or that the rise stops beyond a certain extent; searches for proteolysis and ripening did not establish that pattern. Page numbers were unavailable in our copy. (LLM, conf=0.78)

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  • The presence of active peptides that are naturally formed in cheese depends on a delicate equilibrium between their formation and their degradation by the proteolytic systems involved in cheese ripening.

    “The presence of active peptides that are naturally formed in cheese depends on a delicate equilibrium between their formation and their degradation by the proteolytic systems involved in cheese ripening (Vargas-Bello-Pérez et al., 2019, Guha et al., 2021).”

    From Antioxidant and antihypertensive activity of Gouda cheese at different stages of ripening (2022) · cites this paper as Vargas-Bello-Pérez et al., 2019

    The 'Other factors influencing milk protein composition' section reports that cheese starter and adjunct cultures can increase production of bioactive peptides in cheese. The copy does not say that their presence depends on a balance between formation and degradation by proteolytic systems during ripening; a reference title mentions ripening, but does not establish that mechanism. (LLM, conf=0.83)

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  • Glycan chains from the glycomacropeptide region at the C-terminus of κ-casein may protect against hydrolysis by conferring hydrophilic properties and negative charge, increasing electrostatic repulsions.

    “Glycan chains from the glycomacropeptide region at the C-terminus of κ-casein may protect against hydrolysis in this region because they confer hydrophilic properties and negative charge, increasing electrostatic repulsions”

    From Antioxidant and antihypertensive activity of Gouda cheese at different stages of ripening (2022) · cites this paper as Vargas-Bello-Pérez et al., 2019

    The Animal genetics section mentions glycosylation of milk-protein peptide chains, but does not discuss glycan chains at the C-terminus of κ-casein or protection from hydrolysis. Searches for glycomacropeptide, hydrophilicity, negative charge, and electrostatic repulsion found no passage addressing the proposed mechanism. Page numbers were unavailable in our copy. (LLM, conf=0.72)

    Experimental — accuracy not yet measured
  • αS2-casein could be more resistant to hydrolysis due to the formation of a tetrameric structure, providing protection in some regions.

    “In this sense, αS2-casein could be more resistant to hydrolysis due to the formation of a tetrameric structure, providing protection in some regions.”

    From Antioxidant and antihypertensive activity of Gouda cheese at different stages of ripening (2022) · cites this paper as Vargas-Bello-Pérez et al., 2019

    The Animal genetics section identifies αs2-casein as a milk protein, but does not discuss its resistance to hydrolysis. Searches for a tetrameric structure and protected regions found no passage in our copy addressing the proposed mechanism; the Cancer section instead discusses proteolytic resistance in β-casomorphins. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

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Cites

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Research works printed but not linked: 4

  1. Beltrán-Barrientos LM, Hernández-Mendoza A, Torres Llanez MJ, González-Córdova AF and Vallejo-Córdoba B (2016) Fermented milk as antihypertensive functional food. Journal of Dairy Science 99, 4099-4110.
  2. Hao LY, Wang J, Sun P and Bu DP (2016) The effect of heat stress on the metabolism of dairy cows: updates and review. Austin Journal of Nutrition and Metabolism 3, 10363-11041.
  3. Khatoon JA and Josh VK (1987) Effect of different heat treatments on protease-peptone and non protein nitrogen contents of goat milk. Indian Journal of Dairy Science 40, 243-245.
  4. National Research Council (NRC) (2001) Nutrient Requirements of Dairy Cattle, 7th Edn. Washington, DC: National Academy Press.

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Authors
Vargas-Bello-Pérez, E., Márquez-Hernández, R. I., & Hernández-Castellano, L. E.
Affiliations
  • Universidad Nacional Autónoma de México (MX)
  • Aarhus University (DK)
Corresponding author
Hernández-Castellano, Lorenzo E.
Venue
Journal of Dairy Research
Published
2019-05
Volume
86
Issue
2
Pages
136-144
ISSN
  • 0022-0299 (ISSN-L)
  • 1469-7629
OpenAlex
W2948951493
Cited by
97
References
81
Citations by year
2026: 12 · 2025: 9 · 2024: 13 · 2023: 12 · 2022: 19 · 2021: 15 · 2020: 16 · 2019: 1
FWCI
4.22
Type
journal article
Language
en
Open access
Locations
  • Journal of Dairy Research (publishedVersion)
  • PubMed (publishedVersion)
  • Acceda (Universidad de Las Palmas de Gran Canaria) (submittedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
  • Scopus (Elsevier) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Animal Diversity and Health Studies
Keywords
bioactive peptides, milk protein, animal genetics, animal nutrition, ruminants, alpha-lactalbumin, β-lactoglobulin, casein, in vitro bioactivity
MeSH terms
Animals, Cattle, Humans, Milk, Milk Proteins, Nutritive Value, Functional Food

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