Abstract

Lysozyme has attracted immense attention as an antimicrobial agent because of its ability to lyse the bacterial cell wall. It is found in a wide variety of body fluids and in cells of the innate immune system. Lysozyme can act as muramidase or as a Cationic Antimicrobial Peptide (CAMP). Lysozyme has many applications in the medical and industrial fields. Based on enzyme nomenclature, lysozyme is classified as a glycosylase under the group hydrolases. This manuscript covers a fundamental review of lysozyme in terms of discovery, history, functions and various sources and types of lysozyme. The biological and molecular structure is discussed as well as notable bioengineering and protein modifications. Furthermore, the mechanisms of resistance to lysozyme in microorganisms have also been discussed. Lastly, different methods that have been developed for detecting and measuring the activity of lysozyme are outlined. Although, a recombinant lysozyme has not yet been produced, several studies have attempted to generate a modified lysozyme either for large-scale production or that which is more suitable for industrialization purposes.

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