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Casocidin-I: a casein-alpha s2 derived peptide exhibits antibacterial activity.
Niedersächsisches Institut für Peptid-Forschung (IPF) Hannover, Germany.
Here we report the isolation and characterization of an antibacterial peptide from bovine milk inhibiting the growth of Escherichia coli, and Staphylococcus carnosus. The primary structure of the peptide was revealed as a 39-amino-acid-containing fragment of bovine alpha s2-casein (position 165-203) by means of Edman amino acid sequencing and mass spectrometry. Since human milk does not contain any casein-alpha s2, these findings could explain the different influence of human and bovine milk on the gastrointestinal flora of the suckling.
PMID: 7556666 [PubMed - indexed for MEDLINE]
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Cited by 3 PubMed Central articles
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Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species.
Minervini F, Algaron F, Rizzello CG, Fox PF, Monnet V, Gobbetti M.
Appl Environ Microbiol. 2003 Sep; 69(9):5297-305.
[Appl Environ Microbiol. 2003]
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Kappacin, a novel antibacterial peptide from bovine milk.
Malkoski M, Dashper SG, O'Brien-Simpson NM, Talbo GH, Macris M, Cross KJ, Reynolds EC.
Antimicrob Agents Chemother. 2001 Aug; 45(8):2309-15.
[Antimicrob Agents Chemother. 2001]
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The effects of adding lactococcal proteinase on the growth rate of Lactococcus lactis in milk depend on the type of enzyme.
Helinck S, Richard J, Juillard V.
Appl Environ Microbiol. 1997 Jun; 63(6):2124-30.
[Appl Environ Microbiol. 1997]