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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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
Citations
Cites
Identification of the bactericidal domain of lactoferrin
Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K., & TOMITA, M. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90346-f · Cited by 890
Purification and Characterization of Angiotensin I-Converting Enzyme Inhibitors from Sour Milk
Nakamura, Y., Yamamoto, N., Sakai, K., Ōkubo, A., Yamazaki, S., & Takano, T. (1995) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(95)76689-9 · Cited by 838
The proteotytic systems of lactic acid bacteria
Kunji, E. R. S., Mierau, I., Hagting, A., Poolman, B., & Konings, W. N. (1996) · Antonie van Leeuwenhoek · doi:10.1007/bf00395933 · Cited by 724
Enzymes of the Renin-Angiotensin System and their Inhibitors
Ondetti, M. A., & Cushman, D. W. (1982) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.51.070182.001435 · Cited by 467
Potent Antibacterial Peptides Generated by Pepsin Digestion of Bovine Lactoferrin
TOMITA, M., Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., & Kawase, K. (1991) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(91)78608-6 · Cited by 445
Yamamoto, N., Akino, A., & Takano, T. (1994) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(94)77026-0 · Cited by 418
Maeno, M., Yamamoto, N., & Takano, T. (1996) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(96)76487-1 · Cited by 392
Overview on Milk Protein-derived Peptides
Meisel, H. (1998) · International Dairy Journal · doi:10.1016/s0958-6946(98)00059-4 · Cited by 359
Self-citationAngiotensin I Converting Enzyme Inhibitory Peptides Derived from Bovine Milk Proteins
Pihlanto-Leppälä, A., Rokka, T., & Korhonen, H. J. T. (1998) · International Dairy Journal · doi:10.1016/s0958-6946(98)00048-x · Cited by 355
The physiology and biochemistry of the proteolytic system in lactic acid bacteria
Pritchard, G. G., & Coolbear, T. (1993) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1993.tb00018.x · Cited by 310
Research works printed but not linked: 10
- Daniel H, Wessendorf A, Vohwinkel M & Brantl V (1990b) Effect of D-Ala2,4Tyr5-β-casomorphin-5-amide on gastrointestinal functions. In: Nyberg F & Brantl V (Eds) β-Casomorphins and Related Peptides (pp 95-104). Fyris-Tryck AB, Uppsala
- Fukudome S-I & Yoshikawa M (1994) Isolation and characterizaton of opioid peptides derived from wheat gluten. In: V. Brantl & H. Teschemacher (Eds) β-Casomorphins and related peptides: recent developments (pp 27-33). VCH, Weinheim
- Meisel H & Schlimme E (1994) Inhibitors of Angiotensin-Converting-Enzyme derived from bovine Casein (Casokinins). In: Brantl V & Teschemacher H (Eds) β-Casomorphins and related peptides: recent developments (pp 27-33). VCH, Weinheim
- Meisel H & Schlimme E (1996) Bioactive peptides derived from milk proteins: Ingredients for functional foods? Kieler Milchwirtschaftl. Forschungsber. 48: 343-357
- Pelissier JP (1984) Proteolysis of caseins. Sciences des Aliments 4: 1-35
- Shimizu M (1999) Modulation of intestinal functions by food substances. Nahrung/Food 143: 154-158 · DOI
- Teschemacher H & Brantl V (1994) Milk protein derived atypical opioid peptides and related compounds with opioid antagonist activity. In: Brantl V & Teschemacher H (Eds) β-Casomorphins and Related Peptides: Recent Developments (pp 3-17). VCH, Weinheim
- Teschemacher H, Koch G & Brantl V (1997) Milk protein-derived opioid receptor ligands. Biopoly. 43: 99-117 · DOI
- Yamamoto N (1997) Antihypertensive peptides derived from food proteins. Biopoly. 43: 129-134 · DOI
- Yoshikawa M, Tani F & Chiba H (1988) Structure-activity relationship of opioid antagonist peptides derived from milk proteins. In: Shiba T (Ed) Peptide Chemistry (pp 473-476). Protein Research Foundation, Osaka
Cited by
Sorted by citations
Lactic acid bacteria as functional starter cultures for the food fermentation industry
Leroy, F., & De Vuyst, L. (2004) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2003.09.004 · Cited by 1,852
Bioactive peptides: Production and functionality
Korhonen, H. J. T., & Pihlanto, A. (2006) · International Dairy Journal · doi:10.1016/j.idairyj.2005.10.012 · Cited by 1,822
Metabolism Characteristics of Lactic Acid Bacteria and the Expanding Applications in Food Industry
Wang, Y., Wu, J., Lv, M., Shao, Z., Hungwe, M., Wang, J., Bai, X., Xie, J., Wang, Y., & Geng, W. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.612285 · Cited by 1,001
Hypotensive Peptides from Milk Proteins
Fitzgerald, R. J., Murray, B. A., & Walsh, D. J. (2004) · Journal of Nutrition · doi:10.1093/jn/134.4.980s · Cited by 725
Proteolytic systems of lactic acid bacteria.
Savijoki, K., Ingmer, H., & Varmanen, P. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0427-1 · Cited by 717
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
