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Physicochemical evaluation of preparations obtained as a result of enzymatic modification of lysozyme with pepsin and trypsin
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1  Department of Food Quality and Safety Management, Poznań University of Life Sciences, 60-637 Poznań, Poland
Academic Editor: Arun Bhunia


Lysozyme is a 14.3 kDa protein consisting of 129 amino acids. Modifications of this molecule lead to oligomers and dimers, but more and more attempts are made to break down the lysozyme monomer into smaller molecules. The peptides obtained as a result of these processes can have bioactive properties, thanks to which they can be used in the food, pharmaceutical and medical industries. The aim of the research was to develop a method for the preparation and analytical evaluation of bioactive lysozyme derivatives resulting from enzymatic hydrolytic catalysis of native lysozyme derived from chicken egg white (Leśnierowski G. Eta al. 2012; Leśnierowski G. Eta al. 2020). The modification was carried according to the modified method Carillo W. et al. 2014. The test material was a 3% aqueous solution of commercially available native lysozyme from Belovo (Belgium). The hydrolytic catalysis was carried out with the use of specifically selected proteolytic enzymes, ie trypsin and pepsin. The hydrolysis processes were run for 60 minutes in the Syncore Analyst analytical reactor by Büchi (Switzerland) and the chemical reactor by Eppendorf Thermo Mixer (Germany). The factors differentiating the hydrolysis variants were: pH of the mixture (2, 4, 6) and temperature (40, 55 and 70 ° C). The hydrolysis reactions were stopped by heating the mixture to 80 ° C for a period of 5 min. The effectiveness of the process conditions was assessed by electrophoresis and densitometry. The next stage of the research was to evaluate the hydrolytic, hydrophobic and antioxidant activity of the preparations (Leśnierowski G. et. al. 2012). The conditions for carrying out the lysozyme modification had a significant impact on the electrophoretic separation, as well as on the hydrolytic, hydrophobic and antioxidant activity of the obtained preparations. The highest percentage of peptides was obtained by hydrolysis with pepsin at the temperature of 70 ° C and pH 4. The obtained preparations obtained as a result of the modification are characterized by significantly higher (p <0.05) antioxidant and hydrolytic activity compared to the lysozyme monomer.


Carillo W., Garcia-Ruiz A., Recio I., Moreno-Arribas M.V., 2014: Ancibaterial Activity of Hen Egg White Lysozyme Modified by Heat and Enzymatic Treatments against Oenological Lactic Acid Bacteria and Acetic Acid Bacteria. Journal of Food Protection, 77(10), 1732-1739

Leśnierowski G., Cegielska-Radziejewska R., 2012: Potential possibilities of production, modification and practical application of lysozyme. Acta scientarium polonorum. Technologia alimentarna, 11(3), 223-230

Leśnierowski G., Yang T., 2020: Lysozyme and its modified forms: A critical appraisal of selected properties and potential. Trends in Food Science & Technology, 107, 333-342

Keywords: lysozyme; bioactive peptides; enzymatic hydrolysis; hydrolytic activity; hydrophobic activity; antioxidant activity