Lysozyme has been applied and developed in various industries, and is highly favored and loved. It stands out among over 2000 enzymes. Lysozyme was first discovered by British bacteriologist Fleming in 1922 in human tears and saliva. Due to its ability to resist microorganisms such as bacteria, it is named lysozyme, which means the enzyme that dissolves bacteria.
Lysozyme is a protein defense factor and an important immune factor in animals. It is a hydrolytic enzyme that specifically acts on the cell wall of microorganisms, also known as cell wall lytic enzyme. This enzyme is widely present in various tissues of the human body, including egg white from birds and poultry, tears, saliva, plasma, milk, and other liquids from mammals. Microorganisms also contain this enzyme, with egg white being the most abundant.
According to the different sources of lysozyme, it can be divided into four categories: plant lysozyme, animal lysozyme, microbial lysozyme, and egg white lysozyme.
1.Lysozymes in plants
Currently, lysozyme has been isolated from plants such as papaya, turnips, barley, figs, and cabbage, with a molecular weight of approximately 24000-29000. The activity of plant lysozyme against Streptococcus pyogenes is not more than one-third of that of egg white lysozyme, but its activity in decomposing colloidal chitin is 10 times that of egg white lysozyme.
2.Lysozymes in humans and feeding animals
This enzyme has been found in the tissues and secretions of humans and many feeding animals. It is known that this enzyme is present in human secretions such as tears, nasal mucus, saliva, and R juice, as well as in liver, kidney, and lymphatic tissues. The advanced structure of human lysozyme and egg white lysozyme is very similar, with human lysozyme activity three times higher than egg white lysozyme activity. At present, lysozyme has been isolated from R juice of cattle and horses, and its physicochemical properties are basically similar to human lysozyme, but its structure is not clear, and its lysozyme activity is also much lower than human lysozyme by about 3000 times.
3.Lysozymes produced by microorganisms
There are three types of bacterial cell wall lysozymes: (1) Endo N-acetylhexosaminases: enzymes that destroy peptidoglycans in bacterial cell walls, β- 1,4 glycosidic bonds, similar to the action of egg white lysozyme. (2) Amidase: cleaves the N-acetyl cellwall acid-L-alanine bond between the N-acetyl cellwall acidpeptide tails in bacterial cell wall peptidoglycans. (3) Endopeptidase: capable of breaking peptide bonds within peptide tails and bridges; Existing research has found that the antibacterial activity of bacterial cell lysozyme is not only manifested in its ability to break down bacterial cell walls, but also exhibits antibacterial effects even when the enzyme is irreversibly inhibited; Bacterial cell wall lysozyme from different sources has different antibacterial ranges and specificity for different types of peptidoglycans.
4.Egg white lysozyme
Egg white lysozyme accounts for 3.4%~3.5% of the total protein in egg white, and is a typical representative of lysozyme in animals and plants, and is also one of the most well understood lysozymes currently. Can decompose Gram positive bacteria such as Streptococcus pyogenes, Staphylococcus aureus, and Bacillus megaterium, but ineffective against Gram negative bacteria. When diethylenetriamine is present, certain G-bacteria can also be decomposed by this enzyme. The molecular weight of lysozyme in egg white is 14000, the isoelectric point is 11.1, the optimal temperature is $2, and the optimal pH value is 6-7. Its chemical properties are very stable, and its structure remains stable even when the pH value changes dramatically in the range of 1.2-11.3. It is a thermally stable alkaline protein in acidic environments, but has poor thermal stability in alkaline environments; Within the pH range of 4-7, $2 treatment for 1 minute still maintains the original enzyme activity. Its primary structure is composed of 129 amino acids, and the main forces that maintain its structure are disulfide bonds, hydrogen bonds, and hydrophobic bonds.
Egg white lysozyme, as a typical representative of lysozyme, is a stable protein with an optimal pH of 4-6.5 and an optimal temperature of 35 ℃. The optimal amount of lysozyme added to feed depends on different animals and specific production requirements.
Lysozyme is a kind of protein defense factor, an important immune factor of animals themselves, and a kind of hydrolase which specifically acts on the cell wall of microorganisms, also known as cell wall lytic enzyme. This enzyme widely exists in many tissues of human body, such as egg white of birds and poultry, tears, saliva, plasma, milk and other liquids of mammals, and microorganisms also contain this enzyme, among which egg white is the most abundant.
The information in this article comes from the Internet and is not used as treatment advice or investment advice. If this article has an impact on your rights and interests or is interested in this product, please contact us in time so that we can provide you with more help