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.
Highlights
Lysozyme (1, 4-N-acetylmuramidase, E.C.3.2.1.17) is a small cationic protein first reported by Laschtschenko in 1909 (Burgess, 1973)
Fleming was at the time suffering from a cold and he allowed drops of his nasal secretions to fall onto an agar culture plate that was thickly colonized with bacteria
Lysozyme is a bacteriolytic enzyme that has the ability to hydrolyze glycosidic bonds of 1,4-beta-linkages between N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) in peptidoglycan (PG), which is present in the cell walls of prokaryotes (Mir, 1977; Akinalp et al, 2007) (Figure 1)
Summary
Lysozyme (1, 4-N-acetylmuramidase, E.C.3.2.1.17) is a small cationic protein first reported by Laschtschenko in 1909 (Burgess, 1973). The plates were incubated at a certain temperature for a number of hours, after which radial inhibition beyond the nasal mucus on the plate was observed This experiment was later termed the lysoplate and it was concluded that the nasal secretions contained an enzyme capable of bacterial lysis. With the success of his preliminary experiment, Fleming (1922) continued to work with lysozyme, testing its antibacterial properties with several different bacteria He reported the discovery of a small round bacterium Micrococcus lysodeikticus ( referred to as Micrococcus luteus) which was vulnerable to lysozyme. Wolff (1927) reported on its chemistry; Hoder (1931) its relation to immunology; Anderson (1932) its importance in vitamin A deficiency; Corper (1932) its relation to tuberculosis; Meyer et al (1936a) its purification and properties; and Meyer et al (1936b) combined with Daly (1938) the mechanism of its action It is a paramount component of innate immunity due to its antibacterial, antiviral, www.ccsenet.org/ijb. In the future, the development of advanced technology in molecular biology and fermentation could facilitate large scale production of T4L for industrial and medical purposes
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