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Plasmin digest of κ-casein as a source of antibacterial peptides

Published online by Cambridge University Press:  18 March 2014

Marjaneh Sedaghati ,
Hamid Ezzatpanah ,
Masoud Mashhadi Akbar Boojar ,
Maryam Tajabadi Ebrahimi  and
Mehdi Aminafshar
Marjaneh Sedaghati
Affiliation:
Department of Food Science and Technology, College of Food Science and Technology, Tehran Science and Research Branch, Islamic Azad University, Tehran, Iran
Hamid Ezzatpanah*
Affiliation:
Department of Food Science and Technology, College of Food Science and Technology, Tehran Science and Research Branch, Islamic Azad University, Tehran, Iran
Masoud Mashhadi Akbar Boojar
Affiliation:
Department of Biochemistry, Kharazmi University, Tehran, Iran
Maryam Tajabadi Ebrahimi
Affiliation:
Department of Science, Faculty of Biology, Islamic Azad University, Tehran Central Branch, Iran
Mehdi Aminafshar
Affiliation:
Department of Animal Science and Technology, Faculty of Agriculture and Natural Resources, Tehran Science and Research Branch, Islamic Azad University, Tehran, Iran
*
*For correspondence; e-mail: [email protected]
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Abstract

This study investigated the antibacterial properties of plasmin, the plasmin hydrolysis of bovine κ-casein and the fractions (named κC1, κC2, κC3, κC4, and κC5) liberated from it using RP-HPLC. The target bacteria were Escherichia coli, Staphylococcus aureus (pathogenic), Lactobacillus casei and Lactobacillus acidophilus (probiotic). Three peptides (kC1, kC3, and kC4) were found to have antibacterial activity, with κC3 peptide being the most active. The plasmin digest of bovine κ-casein proved to be stronger than any of its fractions in terms of antibacterial potential. Measurement of the minimum inhibitory concentration (MIC) showed that Gram-positive bacteria are generally more sensitive to antibacterial activity than Gram-negative bacteria. The MIC of nisin, as a bacteriocin peptide, was also measured. The three antibacterial peptides were identified using LC-Mass. The molecular mass of kC1, kC3, and kC4 corresponded to the f(17–21), f(22–24), and f(1–3) of bovine κ-casein, respectively. It was also found that the positive charge and hydrophobicity of a peptide are not key factors in antibacterial activity. On the whole, the present study demonstrated that the plasmin digest of κ-casein has a high antibacterial potential and can be considered as a natural antibacterial agent in the food chain.

Keywords

Bovine milk proteinsκ-caseinantibacterial peptidesplasmin
Type
Research Article
Information
Journal of Dairy Research , Volume 81 , Issue 2 , May 2014 , pp. 245 - 251
Copyright
Copyright © Proprietors of Journal of Dairy Research 2014 

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