Physico-chemical properties and antibacterial activity of modified egg white—lysozyme

Abstract

Lysozyme (N-acetyl-muramyl-hydrolase E.C. 3.2.1.17) is a low-molecular enzyme (14,400 Da) found in body secretions, systemic fluids and tissues of humans and animals. Antibacterial activity of lysozyme monomer is limited first of all to Gram-positive bacteria, which is connected with the structure of the cell wall. This enzyme catalyzes hydrolysis of β-glycoside bonds (1–4), releasing N-acetylglucosamine and N-acetylmuramic acid. The spectrum of antibacterial activity of lysozyme may be extended thanks to modifications of the enzyme. The aim of the study was to assess antibacterial activity, hydrolytic activity and surface hydrophobicity of different forms of lysozyme. Chemical and thermo-chemical modification of lysozyme was performed, and the antibacterial action of lysozyme monomer and modified preparations were compared. It was found that in comparison with monomer and the control, all modified preparations exhibit effective action against Gram (−) bacteria Pseudomonas fluorescens. A particularly effective action was found in case of lysozyme subjected to thermo-chemical modification, which was characterized by the highest proportion of oligomeric forms and the highest hydrophobicity.