Proteolytic fragments of ovalbumin display antimicrobial activity
Ovalbumin, one of the major proteins present in avian egg white, was proteolytically digested by trypsin and chymotrypsin and the peptide fragments were investigated for their antimicrobial activity. The antimicrobial peptides were isolated and characterized. From the tryptic digestion, the followin...
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Published in: | Biochimica et biophysica acta Vol. 1672; no. 2; pp. 76 - 85 |
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Main Authors: | , , , |
Format: | Journal Article |
Language: | English |
Published: |
Netherlands
Elsevier B.V
03-05-2004
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Subjects: | |
Online Access: | Get full text |
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Summary: | Ovalbumin, one of the major proteins present in avian egg white, was proteolytically digested by trypsin and chymotrypsin and the peptide fragments were investigated for their antimicrobial activity. The antimicrobial peptides were isolated and characterized. From the tryptic digestion, the following five antimicrobial peptide fragments were obtained: SALAM (residues 36–40), SALAMVY (residues 36–42) YPILPEYLQ (residues 111–119), ELINSW (residues 143–148) and NVLQPSS (residues159–165). Digestion of ovalbumin by chymotrypsin yielded the antimicrobial peptides AEERYPILPEYL (residues 127–138), GIIRN (residues 155–159) and TSSNVMEER (residues 268–276). The peptides were synthesized and found to exert antimicrobial activity. They were strongly active against
Bacillus subtilis and to a lesser extent against the other bacterial strains examined. A weak fungicidal activity against
Candida albicans was also shown by some peptides. Ovalbumin itself was not bactericidal against all the bacteria strains examined. Our results suggest that the food protein ovalbumin may supply the organism with antimicrobial peptides, supporting the immunodefences of the organism. |
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ISSN: | 0304-4165 0006-3002 1872-8006 |
DOI: | 10.1016/j.bbagen.2004.02.010 |