Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.17 extracted from

  • Liburdi, K.; Straniero, R.; Benucci, I.; Vittoria Garzillo, A.M.; Esti, M.
    Lysozyme immobilized on micro-sized magnetic particles: kinetic parameters at wine pH (2012), Appl. Biochem. Biotechnol., 166, 1736-1746.
    View publication on PubMed

Application

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

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 [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

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Gallus gallus
-
-
soluble
-
Gallus gallus
-
-

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Gallus gallus
-
egg white
-
Gallus gallus
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
LYZ
-
Gallus gallus
peptidoglycan n-acetylmuramic hydrolase
-
Gallus gallus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Gallus gallus

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
-
Gallus gallus

General Information

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