[Immobilization of urease from Staphylococcal saprophyticus L-1 on activated silica].
The paper deals with immobilization of urease obtained from Staphylococcus saprophyticus L-1 on the organic silica surfaces. The process completion time (4-5 h) and the optimal pH of binding (7-8) are practically independent of the chemical nature of the carrier surface. The value of the specific activity of urease grafted to silica depends not only on the type of the enzyme-carrier bond, but also on the macromolecule protein-to-silica distance. The extent of the retained enzyme activity is shown to be 26% after sorption on the initial silica. It grows to 100% with an increase of the organic radical length which separates the biocatalyst and the carrier.
Liubinskiĭ
G V
GV
Ianishpol'skiĭ
V V
VV
Tertykh
V A
VA
Iuodval'kite
D Iu
DIu
Glemzha
A A
AA
D055598:Chemical Phenomena; D002621:Chemistry; D004800:Enzymes, Immobilized / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D012822:Silicon Dioxide; D013210:Staphylococcus / Q000201:enzymology*; D014510:Urease / Q000302:isolation & purification*
D004800:Enzymes, Immobilized; D012822:Silicon Dioxide; D014510:Urease
Immobilizatsiia ureazy is Staphylococcus saprophyticus L-1 na aktivirovannykh kremnezemakh.