Discovery, Modification and Production of T4 Lysozyme for Industrial and Medical Uses
Author(s) -
Alaa Alhazmi,
Johnathan Warren Stevenson,
Samuel Amartey,
Wensheng Qin
Publication year - 2014
Publication title -
international journal of biology
Language(s) - English
Resource type - Journals
eISSN - 1916-968X
pISSN - 1916-9671
DOI - 10.5539/ijb.v6n4p45
Subject(s) - lysozyme , antimicrobial , muramidase , lysis , enzyme , antimicrobial peptides , chemistry , biology , biochemistry , microbiology and biotechnology , computational biology
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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