Application | Comment | Organism |
---|---|---|
food industry | possible use of lysozyme as an anti-microbial agent during the winemaking process, the enzyme is covalently immobilized on two different micro-size magnetic particles, the tosyl-activated particles are more stable, overview. The insoluble lysozyme provides advantages over the soluble form, such as enabling reutilization of enzyme and an increase in stability, immobilization may impart stable antimicrobial capability to the surface of food packaging polymers and create a more suitable microenvironment for the enzyme. Treated food can be claimed additive-free following removal of immobilized lysozyme | Gallus gallus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | covalent immobilization of the enzyme on two different micro-size magnetic particles, i.e. tosyl-activated and carboxylated, at pH 3.2, 37°C for 20 h under rotation | Gallus gallus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics with cell suspension of Oenococcus oeni at pH 3.2 and pH 4.5 of free and immobilized enzyme, overview | Gallus gallus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Gallus gallus | - |
- |
soluble | - |
Gallus gallus | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gallus gallus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Gallus gallus | - |
egg white | - |
Gallus gallus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | a commercial cell suspension of Oenococcus oeni, an oenological strain involved in the winemaking process, is utilized as enzyme substrate | Gallus gallus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LYZ | - |
Gallus gallus |
peptidoglycan n-acetylmuramic hydrolase | - |
Gallus gallus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Gallus gallus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
pH 3.2, half-life for the free enzyme is 39 h, for the enzyme immobilized on tosyl-activated and carboxylated micro-size magnetic particles is 280 h and 134 h, respectively | Gallus gallus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.5 | - |
- |
Gallus gallus |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme causes cell lysis by cleaving the beta-(1-4) glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine in the peptidoglycan layer of Gram-positive bacteria | Gallus gallus |