Abstract

BackgroundLysozyme is present in most organisms in the world, in which it performs highly important protective biological functions. The native form of this enzyme is a monomer that destroys Gram-positive bacteria by breaking the glycosidic bonds β(1–4); in its dimeric form, which is achieved after modification of the monomer, it gains completely new valuable properties, such as bacteriostatic activity against Gram-negative bacteria and medical properties. Such properties are exhibited by lysozyme from every known source, including chicken egg white, which can be commercially obtained. Native lysozyme obtained from hen egg white (HEWL) and its modified forms have highly valuable protective properties, particularly in food storage but also in other areas, such as medicine, pharmacology and veterinary medicine. Scope and approachIn this review, the basic properties of the native lysozyme of chicken egg whites are characterized, and new research findings are shown. This review introduces the main methods of isolating and modifying this enzyme, as well as the practical uses of various forms of this protein. This work also highlights the importance of conducting further research on the modification of lysozyme in order to fully realize its potential.Key Findings and Conclusion: The lysozyme monomer is a natural agent that exhibits powerful antimicrobial properties. Against Gram-positive bacteria. As a result of specific modifications that change the structure of the lysozyme molecule, however, the potential of the enzyme increases significantly. The presented methods, including entirely new methods, enable the transformation of lysozyme into a new oligomeric form of the enzyme (with different degrees of oligomerization and different hydrophobicity) with new properties, including action against Gram-negative bacteria, viruses and other microorganisms. New possibilities for the use of this form of lysozyme in the food industry, as well as in medicine and veterinary medicine, are discussed.

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