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Thermally and chemical-thermally modified lysozyme and its bacteriostatic activity

Published online by Cambridge University Press:  18 September 2007

G. Lesnierowski ,
R. Cegielska-Radziejewska  and
J. Kijowski
G. Lesnierowski*
Affiliation:
Department of Food Quality Management, A. Cieszkowski Agricultural University, Wojska Polskiego 31, 60-624 Poznań, Poland
R. Cegielska-Radziejewska
Affiliation:
Department of Food Quality Management, A. Cieszkowski Agricultural University, Wojska Polskiego 31, 60-624 Poznań, Poland
J. Kijowski
Affiliation:
Department of Food Quality Management, A. Cieszkowski Agricultural University, Wojska Polskiego 31, 60-624 Poznań, Poland
*
*Corresponding author: e-mail: lesnier@au.poznan.pl
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Abstract

Our investigations indicated a possibility to extend the range of lysozyme activity using thermal and chemical – thermal modification. We found that under the adopted conditions of modification a weakly acid environment (pH 5 – 6) promotes an increased polymerisation of lysozyme and makes it possible to obtain approx. 50% of polymers. It was observed that lysozyme concentration in the solution subjected to thermal modification, the pH value of the solution, the temperature and time of modification have a significant effect on the content of the forming polymers. It was found that the application of lysozyme modification leads to an increase in its antibacterial activity in a comparison to the activity of lysozyme monomer. The modified lysozyme did reduce viability of Gram-positive bacteria and Gramnegative bacteria.

Keywords

lysozymemonomerdimermodificationhydrolytic activitybacteriostatic activity

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Type
Reviews
Information
World's Poultry Science Journal , Volume 60 , Issue 3 , September 2004 , pp. 303 - 310
Copyright
Copyright © Cambridge University Press 2004

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References

Ibrahim, H.R., Kato, A. and Kobayashi, K. (1991) Antimicrobial effects of lysozyme against Gramnegative bacteria due to covalent binding of palmitic acid. Journal of Agricultural and Food Chemistry 39: 2077–2082.CrossRefGoogle Scholar
Ibrahim, H.R., Yamada, M., Matsushita, K., Kobayashi, K. and KATO, A. (1994) Enhanced bactericidal action of lysozyme to Escherichia coli by inserting a hydrophobic pentapeptide into C Terminus. Journal of Biological Chemistry 269: 5059–5063.CrossRefGoogle ScholarPubMed
Ibrahim, H.R., Higashiguchi, S., Juneja, L.R., Kim, M. and Yamamoto, T. (1996) A structural phase of heat–denatured lysozyme with novel antimicrobial action. Journal of Agricultural and Food Chemistry 44: 1416–1423.CrossRefGoogle Scholar
Ibrahim, H.R., Higashiguchi, S., Sugimoto, Y. and AOKI, T. (1997) Role of divalent cations in the novel bactericidal activity of the partially unfolded lysozyme. Journal of Agricultural and Food Chemistry 45: 89–94.CrossRefGoogle Scholar
Ibrahim, H.R., Aoki, T. and Pellegrni, A. (2002) Strategies for new antimicrobial proteins and peptides: Lysozyme and aprotinin as a model molecules. Current Pharmaceutical Design 8: 671–693.CrossRefGoogle ScholarPubMed
Kato, A., Nakamura, S., Ibrahim, H., Matsumi, T., Tsumiyama, C. and Kato, M. (1998) Production of genetically modified lysozymes having extreme heat stability and antimicrobial activity against Gram negative bacteria in yeast and in plant. Nahrung 42: 128–130.3.3.CO;2-Q>CrossRefGoogle ScholarPubMed
Kijowski, J. and Lesnierowski, G. (1995) The use of lysozyme for food preservation and in medical diagnosis and pharmacology. Biotechnologia 2: 130–140 (in Polish).Google Scholar
Kijowski, J., Lesnierowski, G. and Fabisz-Kijowska, . (2000) Lysozyme polymer formation and functionality of residuals after lysozyme extraction. In: Egg Nutrition and Biotechnology (Sim, J.S., Nakai, S., Guenter, W. Eds.) CAB International, Wallingford, UK, pp. 269–285.Google Scholar
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.CrossRefGoogle ScholarPubMed
Lesnierowski, G. (1997) Isolation of lysozyme from hen egg white using the crystallization, ultrafiltration and ion exchange methods. Diss., Agr. Univ. Poznań, (in Polish).Google Scholar
Lesnierowski, G. and Kijowski, J. (1995) Methods of investigating enzymatic activity and quantitative determination of lysozyme from hen egg white. Przemysl Spozywczy 12: 476–480 (in Polish, abstract in English).Google Scholar
Lesnierowski, G. and Kijowski, J. (2001) Isolation of lysozyme from hen egg white by ion-exchange techniques and its spray drying dehydratation. Polish Journal of Food and Nutrition Sciences 2: 43–47.Google Scholar
Pellegrini, A., Thomas, U., Von Fellenberg, R. and Wild, P. (1992) Bactericidal activities of lysozyme and aprotinin against Gram-negative and Gram-positive bacteria related to their basic character. Journal of Applied Bacteriology 72: 180–187.CrossRefGoogle ScholarPubMed
Proctor, V.A. and Cunnigham, F.E. (1988) The chemistry of lysozyme and its use as a food preservative and a pharmaceutical. Critical Reviews in Food Science and Nutrition 26: 359–395.CrossRefGoogle ScholarPubMed