Physicochemical Evaluation of Preparations Obtained as a Result of Enzymatic Modification of Lysozymes with Pepsin and Trypsin

Abstract

A lysozyme is a 14.3 kDa protein consisting of 129 amino acids. The modification of these molecules leads to oligomers and dimers, but more and more attempts are being made to break down lysozyme monomers 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 this research was to develop a method for the preparation and analytical evaluation of bioactive lysozyme derivatives resulting from the enzymatic hydrolytic catalysis of native lysozymes derived from chicken egg white. The factors differentiating the hydrolysis variants were enzymes (pepsin and trypsin), the pH of the mixture (2, 4, 6), and temperature (40, 55 and 70 °C). The conditions for carrying out lysozyme modification had a significant impact on 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 at 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 monomers.

Keywords

• lysozyme
• bioactive peptides
• enzymatic hydrolysis
• hydrolytic activity
• hydrophobic activity
• antioxidant activity