The DOI matches its Crossref record; 68 of the 71 references it cites were found in a registry or an index.
Bioactive peptides encrypted in milk proteins: proteolytic activation and thropho-functional properties.
Abstract
The bioactivities of peptides encrypted in major milk proteins are latent until released and activated by enzymatic proteolysis, e.g. during gastrointestinal digestion or food processing. The proteolytic system of lactic acid bacteria can contribute to the liberation of bioactive peptides. In vitro, the purified cell wall proteinase of Lactococcus lactis was shown to liberate oligopeptides from beta- and alpha-caseins which contain amino acid sequences present in casomorphins, casokinines, and immunopeptides. The further degradation of these peptides by endopeptidases and exopeptidases of lactic acid bacteria could lead to the liberation of bioactive peptides in fermented milk products. However, the sequences of practically all known biologically active peptides can also be cleaved by peptidases from lactic acid bacteria. Activated peptides are potential modulators of various regulatory processes in the body: Opioid peptides are opioid receptor ligands which can modulate absorption processes in the intestinal tract, angiotensin-I-converting enzyme (ACE)-inhibitory peptides are hemodynamic regulators and exert an antihypertensive effect, immunomodulating casein peptides stimulate the activities of cells of the immune system, antimicrobial peptides kill sensitive microorganisms, antithrombotic peptides inhibit aggregation of platelets and caseinophosphopeptides may function as carriers for different minerals, especially calcium. Bioactive peptides can interact with target sites at the luminal side of the intestinal tract. Furthermore, they can be absorbed and then reach peripheral organs. Food-derived bioactive peptides are claimed to be health enhancing components which can be used for functional food and pharmaceutical preparations.
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In the citing paper
“Milk proteins are considered to be the most important source of bioactive peptides that can be released through hydrolysis by proteolytic microorganisms such as L. helvetius (Meisel and Bockelmann, 1999; Matar et al., 2001; LeBlanc et al., 2002; Fitzgerald and Meisel, 2003; Kenny et al., 2003; de Moreno de LeBlanc et al., 2005).”
From Lactobacillus helveticus: the proteolytic system (2013) · cites this paper as Meisel and Bockelmann, 1999
In the citing paper
“most bioactive peptides are released into the external environment only when cells undergo autolysis, because only occasionally the longer peptides (originated by the first hydrolytic step) possess biological activity (Meisel and Bockelmann, 1999).”
From Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines (2016) · cites this paper as Meisel and Bockelmann, 1999
In the citing paper
“Alpha s1 casein and K-casein hydrolysis gives rise to isracidin and k-casecidin, respectively (McCann et al., 2006). Both peptides display inhibitory action on S. aureus growth (Meisel and Bockelmann, 1999; Atanasova et al., 2014).”
From Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines (2016) · cites this paper as Meisel and Bockelmann, 1999
In the citing paper
“Milk-derived peptides such as the C-terminus sequence of beta casein (193–209) can increase proliferation of rat lymphocytes (Meisel and Bockelmann, 1999)”
From Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines (2016) · cites this paper as Meisel and Bockelmann, 1999
In the citing paper
“beta-casomorphin 7 is opioid, hypotensive, and immunomodulatory: this last function is targeted on lymphocyte proliferation that is sometimes stimulated and sometimes inhibited depending on the peptide concentration (Meisel and Bockelmann, 1999).”
From Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines (2016) · cites this paper as Meisel and Bockelmann, 1999
In the citing paper
“The reason of these mixed functions lies in the fact that some regions in the primary structure of caseins contain overlapping peptide sequences, exerting different physiological functions (Meisel and Bockelmann, 1999). These domains, highly hydrophobic and rich in proline residues, have been defined as “strategic zones” and are resistant to proteolytic attack (Fiat and Jollès, 1989).”
From Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines (2016) · cites this paper as Meisel and Bockelmann, 1999
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Metadata
- Authors
- Meisel, H., & Bockelmann, W.
- Affiliations
- Christian-Albrechts-Universität zu Kiel (DE)
- ORCID
- Bockelmann, Wilhelm
- Venue
- Antonie van Leeuwenhoek
- Published
- 1999-11
- Volume
- 76
- Issue
- 1-4
- Pages
- 207-215
- ISSN
- 0003-6072 (ISSN-L)
- 1572-9699
- OpenAlex
- W1542111917
- Cited by
- 284
- References
- 71
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 4 · 2023: 1 · 2022: 8 · 2021: 9 · 2020: 16 · 2019: 11 · 2018: 12 · 2017: 9 · 2016: 11 · 2015: 18 · 2014: 12 · 2013: 14 · 2012: 12
- FWCI
- 2.41
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Antonie van Leeuwenhoek (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › 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 › Probiotics and Fermented Foods
- Keywords
- bioactive peptides, milk protein, enzymatic proteolysis, lactic acid bacteria, Lactococcus lactis, casein, casomorphins, immunogenic peptides, opioid peptides, ACE inhibitory peptides, immunomodulating peptides, antimicrobial peptides, antithrombotic peptides, caseinophosphopeptides, calcium absorption, fermented milk, functional foods, gastrointestinal digestion
- MeSH terms
- Amino Acid Sequence, Animals, Gram-Positive Bacteria, Humans, Intestinal Absorption, Milk Proteins, Molecular Sequence Data, Peptide Fragments, Endopeptidases, Lactococcus, Lactic Acid
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