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Antibacterial activity of casein-derived peptides isolated from rabbit (Oryctolagus cuniculus) milk

Published online by Cambridge University Press:  09 May 2003

Maria Baranyi
Affiliation:
Agricultural Biotechnology Center, Szent-Györgyi A. 4, H-2100 Gödöllő, Hungary
Ursula Thomas
Affiliation:
Institute of Veterinary Physiology, University of Zurich, Winterthurerstrasse 260, CH-8057 Zurich, Switzerland
Antonio Pellegrini
Affiliation:
Institute of Veterinary Physiology, University of Zurich, Winterthurerstrasse 260, CH-8057 Zurich, Switzerland

Abstract

Acid-precipitated rabbit ‘whole casein’ was digested by trypsin, chymotrypsin, pepsin, and clostripain to screen for possible peptides with antibacterial properties. The peptide fragments were separated by reversed-phase chromatography. The collected fractions were pooled and their antibacterial properties tested against Escherichia coli, Bacillus subtilis and Staphylococcus lentus. Three antibacterial peptide fragments derived from tryptic digestion of rabbit casein were isolated and identified. Their sequences were found as follows: HVEQLLR (residues 50–56 of β-casein), ILPFIQSLFPFAER (residues 64–77 of β-casein), and FHLGHLK (residues 19–25 of αs1-casein). The three peptides were synthesized and found to exert antibacterial effect against Gram positive bacteria only. Proteolytic digestion of rabbit casein by chymotrypsin, pepsin and clostripain yielded several peptide fragments with antibacterial activity. Since antibiotic peptides can be released from casein during the digestion of milk proteins, our results suggest a possible antibacterial function of rabbit caseins. It is conceivable that antibacterial peptides can be generated by endopeptidases of the mammalian gastrointestinal tract possibly providing protection for new-born rabbits against aggression of micro-organisms.

Type
Research Article
Copyright
Proprietors of Journal of Dairy Research 2003

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