PRODUCTS

LYSOZYME

CAS NUMBER: 9001-63-2

EC NUMBER: 232-620-4

MOLECULAR FORMULA: C125H196N40O36S2

MOLECULAR WEIGHT: 2899.3

Lysozyme, also known as muramidase or N-acetylmuramide glycanhydrolase, is an antimicrobial enzyme produced by animals that forms part of the innate immune system.
Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.

This hydrolysis in turn compromises the integrity of bacterial cell walls causing lysis of the bacteria.
Lysozyme is abundant in secretions including tears, saliva, human milk, and mucus.

Lysozyme is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs).
Large amounts of lysozyme can be found in egg white.

Lysozyme is closely related to alpha-lactalbumin in sequence and structure, making them part of the same glycoside hydrolase family 22.
In humans, the C-type lysozyme enzyme is encoded by the LYZ gene.

Hen egg white lysozyme is thermally stable, with a melting point reaching up to 72 °C at pH 5.0.
However, lysozyme in human milk loses activity very quickly at that temperature.

Hen egg white lysozyme maintains its activity in a large range of pH (6-9).
Lysozyme's isoelectric point is 11.35.
The isoelectric point of human milk lysozyme is 10.5-11.

Function and Mechanism:
The enzyme functions by hydrolyzing glycosidic bonds in peptidoglycans.
The enzyme can also break glycosidic bonds in chitin, although not as effectively as true chitinases

Lysozyme's active site binds the peptidoglycan molecule in the prominent cleft between its two domains.
Lysozyme attacks peptidoglycans (found in the cell walls of bacteria, especially Gram-positive bacteria), its natural substrate, between N-acetylmuramic acid (NAM) and the fourth carbon atom of N-acetylglucosamine (NAG).

Shorter saccharides like tetrasaccharide have also shown to be viable substrates but via an intermediate with a longer chain.
Chitin has also been shown to be a viable lysozyme substrate.
Artificial substrates have also been developed and used in lysozyme.

Inhibition:
Imidazole derivatives can form a charge-transfer complex with some residues (in or outside active center) to achieve a competitive inhibition of lysozyme.
In Gram-negative bacteria, the lipopolysaccharide acts as a non-competitive inhibitior by highly favored binding with lysozyme.

Chemical Synthesis:
The first chemical synthesis of a lysozyme protein was attempted by Prof. George W. Kenner and his group at the University of Liverpool in England.
This was finally achieved in 2007 by Thomas Durek in Steve Kent's lab at the University of Chicago who made a synthetic functional lysozyme molecule.

Other Applications:
Lysozyme crystals have been used to grow other functional materials for catalysis and biomedical applications.
Lysozyme is a commonly used enzyme for lysing gram positive bacteria.

Due to the unique function of lysozyme in which it can digest the cell wall and causes osmotic shock (burst the cell by suddenly changing solute concentration around the cell and thus the osmotic pressure), lysozyme is commonly used in lab setting to release proteins from bacterium periplasm while the inner membrane remains sealed as vesicles called the spheroplast.
For example, E. coli can be lysed using lysozyme to free the contents of the periplasmic space.

Lysozyme is especially useful in lab setting for trying to collect the contents of the periplasm.
Lysozyme treatment is optimal at particular temperatures, pH ranges, and salt concentrations.

Lysozyme activity increases with increasing temperatures, up to 60 degrees Celsius, with a pH range of 6.0-7.0.
The salts present also affect lysozyme treatment, where some assert inhibitory effects, and others promote lysis via lysozyme treatment.

Sodium chloride induces lysis, but at high concentrations, it is an active inhibitor of lysis.
Similar observations have been seen with the use of potassium salts.
Slight variations are present due to differences in bacterial strains.

Lysozyme is a hydrolytic enzyme that is present in body fluids such as serum, saliva, gastric juice, milk, and airway mucus secretions
Lysozyme occurs naturally in egg white, but the purified enzyme is used on occasion as an additive in other foods, especially soft cheeses.

Lysozyme, enzyme found in the secretions (tears) of the lacrimal glands of animals and in nasal mucus, gastric secretions, and egg white.
Lysozyme is a special enzyme found in tears, saliva, sweat, and other body fluids.

Other mucosal linings, such as the nasal cavity, also contain lysozyme.
Lysozyme destroys bacteria that attempt to enter our body through these passageways.
In the case of tears, they protect our eyes from bacterial invaders.

Lysozyme was the famous scientist Alexander Fleming who discovered lysozyme in the early twentieth century.
While growing a bacterial culture, a drop of mucus from his nose fell into the culture.

Eventually, he noticed that the bacteria in this culture had been killed.
He named the substance lysozyme by combining two words: 'lyse' and 'enzyme'.

Lysozyme is capable of breaking the chemical bonds in the outer cell wall of the bacteria.
Bacterial cell walls contain a layer of peptidoglycan, which is the specific site that lysozyme targets.

The peptidoglycan layer contains alternating molecules called N-acetylglucosamine and N-acetylmuramic acid.
These molecules form a strong glycan chain that act as the backbone for the cell wall. The link between the N-acetylglucosamine and N-acetylmuramic acid is cleaved by lysozyme.

Lysozyme is a basic bacteriolytic protein that hydrolyzes peptidoglycan and is present in egg white and in human tears and saliva
Lysozyme is an enzyme that is destructive of bacteria and functions as an antiseptic, found in tears, leukocytes, mucus, egg albumin, and certain plants.

Lysozyme is an enzyme found in egg whites and other animal products that demonstrates antibacterial behavior by causing cell lysis in a number of bacterial species
Lysozyme acts as a non-specific defense against bacteria and fungi.

Lysozyme is a component of the innate immune system, and is an important part of an infant's diet to ward off diarrhea.
Lysozyme is an enzyme known for its ability to degrade the polysaccharide architecture of many kinds of cell walls, normally for the purpose of protection against bacterial infection

Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Lysozyme that is encoded in the genome of human.

Lysozyme is a basic enzyme that is present in saliva, tears, egg white, and many animal fluids.
Lysozyme functions as an antibacterial agent.

The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.
Lysozyme is a linear polypeptide obtained from hens' egg whites consisting of 129 amino acids.

Lysozyme possesses enzymatic activity in its ability to hydrolyse the β(1-4) linkages between N-acetylmuramic acid and N-acetylglucosamine in the outer membranes of bacterial species, in particular gram-positive organisms.
Lysozyme is usually obtained as the hydrochloride

PHYSICAL PROPERTIES:

-Molecular Weight: 2899.3

-XLogP3-AA: -12.1

-Exact Mass: 2898.4210899

-Monoisotopic Mass: 2897.4177351

-Topological Polar Surface Area: 1280 Å²

-Physical Description: White, odourless powder having a slightly sweet taste

-Color: White

-Form: powder

-Odour: odourless

-pH: Between 3,0 and 3,6

Lysozyme Occurs in specific granules of human polymorphonuclear leukocytes and takes part in antibacterial activity of leukocytes.
Lysozymes participates in the defense mechanism.

Lysozyme has the ability to stimulate catalysis by bringing steric stress in the substrates.
Lysozyme from human neutrophils has been used in the checkerboard method for establishing a synergy between peptidomimetic 1 and immune effector molecules against E. coli.

CHEMICAL PROPERTIES:

-Heavy Atom Count: 203

-Formal Charge: 0

-Complexity: 6500

-Isotope Atom Count: 0

-Defined Atom Stereocenter Count: 22

-Undefined Atom Stereocenter Count: 0

-Defined Bond Stereocenter Count: 0

-Undefined Bond Stereocenter Count: 0

-Covalently-Bonded Unit Count: 1

-Compound Is Canonicalized: Yes

-Hydrogen Bond Donor Count: 46

-Hydrogen Bond Acceptor Count: 44

-Rotatable Bond Count: 99

Lysozyme treatment is optimal at particular temperatures, pH ranges, and salt concentrations.
Lysozyme activity increases with increasing temperatures, up to 60 degrees Celsius, with a pH range of 6.0-7.0.

Lysozyme is a naturally occurring enzyme found in bodily secretions such as tears, saliva, and milk.
Lysozyme functions as an antimicrobial agent by cleaving the peptidoglycan component of bacterial cell walls, which leads to cell death.
Lysozyme is a hydrolytic enzyme that is present in body fluids such as serum, saliva, gastric juice, milk, and airway mucus secretions

Lysozyme occurs naturally in egg white, but the purified enzyme is used on occasion as an additive in other foods, especially soft cheeses.
Lysozyme, enzyme found in the secretions (tears) of the lacrimal glands of animals and in nasal mucus, gastric secretions, and egg white.

Lysozyme is a special enzyme found in tears, saliva, sweat, and other body fluids.
Lysozyme is a basic bacteriolytic protein that hydrolyzes peptidoglycan and is present in egg white and in human tears and saliva

Lysozyme is an enzyme that is destructive of bacteria and functions as an antiseptic, found in tears, leukocytes, mucus, egg albumin, and certain plants.
Lysozyme is an enzyme found in egg whites and other animal products that demonstrates antibacterial behavior by causing cell lysis in a number of bacterial species
Lysozyme acts as a non-specific defense against bacteria and fungi.

Lysozyme is a basic enzyme that is present in saliva, tears, egg white, and many animal fluids.
Lysozyme functions as an antibacterial agent.

SYNONYMS:

Glycanhydrolase, N-Acetylmuramide
Leftose
Lysozyme
Muramidase
N Acetylmuramide Glycanhydrolase
N-Acetylmuramide Glycanhydrolase
Muramidase
Globulin G1
LYSOZYM
globuling
lysozymeg
Antalzyme
delvozyme
Aids072619
Lysozyme c
Lydium-KLP
globuling1
MURAMIDASE
EC 3.2.1.17
mucopeptide
Heneggwhite
EGGLYSOZYME
Aids-072619
HUMANLYSOZYME
IUB: 3.2.1.17
LYSOZYME, HUMAN
LYSOZYME TYPE VI
Glycanlhydrolase
N-Acetylmuramide
(Amide-d)lysozyme
lysosyme chloride
LYSOZYME GRADE III
LYSOZYME, EGG WHITE
MURAMIDASE GRADE III
n,o-diacetylmuramidase
1,4-N-Acetylmuramidase
1,4-β-N-Acetylmuramidase
β-1,4-N-Acetylmuramidase
mucopeptideglucohydrolase
N-ACETYLMURAMYL HYDROLASE
MUCOPEPTIDE-GLYCOHYDROLASE
CHICKEN EGG WHITE LYSOZYME
LYSOZYME, HUMAN NEUTROPHIL
LYSOZYME GRADE VI: CHLORIDE
MUCOPEPTIDE GLYCOLHYDROLASE
LYSOZYME (CHICKEN EGG WHITE)
lysozymefromhumanneutrophils
MURAMIDASE GRADE VI: CHLORIDE
REDUCED LYSOZYME, WATER SOLUBLE
L1,4-.beta.-N-Acetylmuramidase c
N-acetylmuramide glycanohydrolase
N-Acetylmuramylhydrolase.E.C.3.2.1.17
MUCOPEPTIDE N-ACETYLMURAMOYLHYDROLASE
PEPTIDOGLYCAN N-ACETYLMURAMOYLHYDROLASE
MUCOPEPTIDE N-ACETYLMURAMOYLHYDROLASE GRADE III