Lysozyme (Lz) is an enzyme of 129 amino acids found in tears, nasal secretions, animal tissues, organs, and serum as well as milk and cervical mucus. The major commercial source of Lz is avian egg white and constitutes about 0.5 % of egg albumin. Lysozyme attacks the cell wall polysaccharides of different bacterial species, especially gram positive infectious organisms such as Staphylococci and Streptococci species and kills them. Gram negative bacterial species such as E.coli and Salmonella are also destroyed by Lz, however, they are not as susceptible as Gram positive bacteria. In humans, Lz is used to treat both viral and bacterial infections.
It has analgesic properties and has been used to potentiate antibiotic therapy. EDTA-tris-lysozyme solutions are effective in the treatment of coliform infections of the bladder in humans. Other benefits of Lz is that it neutralizes acIdic substances released during inflammatory processes and so demonstrates anti inflammatory activity. It also helps in wound healing, phagocytosis and regression of degenerative and necrotic process. Lysozyme-mediated decrease of mast cell degranulation leads to reduction of histamine release and a subsequent anti-edema effect.
It has been suggested that polysaccharides, glycopropteins and glycolipids of the cell membrane can bind Lz in a substrate-specific way. This has led to the hypothesis that Lz has a regulatory function in membrane-dependent cellular processes and in protection against membrane abnormalities associated with neoplastic transformation.
In human investigations, fifteen full-term and 18 premature infants were given egg-white Lz in the milk formula (10 mg/100 ml) from the 1st to the 8th week of age as substitute for the Lz in breast milk (2mg/ml) to stimulate the production of immunoglobins. Thirteen full-term and thirteen premature artificially-fed infants, as well as 20 breast-fed infants, were followed as controls.
Assuming that the infants consumed daily 600-900 ml of milk formula, daily intake of Lz in this study was 60-90 mg. The infants did not show ill-effects. No difference in the production of serum immunoglobulin’s between the Lz group and control group was seen. Secretory IgA was found in stool filtrates of full-term Lz fed infants as well as in breast-fed controls.
In other groups, full-term controls fed artificially without lysozyme, premature controls fed artificially with Lz, only traces of secretory IgA were detected in stool filtrates. Lysozyme feeding partly substituted for passive transfer of secretory IgA from maternal milk. No anitbodies were found in serum of Lz fed children thus indicating the safe use of Lz for humans.
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