Properties of the glycoprotein laccase immobilized by two methods.
Laccase (p-diphenol:oxygen oxidoreductase; EC 1.10.3.2) from Neurospora crassa has been immobilized by two different procedures: (1) Covalent attachment to Sepharose 4B activated with cyanogen bromide, and (2) Adsorption to Concanavalin A-Sepharose via the carbohydrate moiety. Except for small changes in the Michaelis-Menten constants, no differences were noted in the enzymological properties of the immobilized enzymes when compared to free enzyme. The carbohydrate moiety of laccase involved in the interaction with Concanavalin A does not appear to be closely associated with the active center since binding to the lectin has no effect on the enzymological parameters investigated.
D004156:Catechol Oxidase / Q000378:metabolism; D003208:Concanavalin A; D003488:Cyanogen Bromide; D004789:Enzyme Activation; D006139:Guaiacol; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009492:Neurospora crassa / Q000201:enzymology; D010101:Oxygen Consumption; D011485:Protein Binding; D012685:Sepharose
D003208:Concanavalin A; D006139:Guaiacol; D012685:Sepharose; D004156:Catechol Oxidase; D003488:Cyanogen Bromide