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EC Number
General Stability
Reference
crystal crosslinking with glutaraldehyde yields a chloroperoxidase preparation with enhanced thermal resistance compared to soluble enzyme
stability studies on the chloroperoxidase complexes in presence of tert-butyl hydroperoxide
the enzyme tolerates up to 30% v/v 1,3-dimethylimidazolium methylsulfate or 1-butyl-3-methylimidazolium methylsulfate
di(ethylene glycol) and di(propylene glycol) stabilize the enzyme towards denaturation by H2O2
immobilization of the enzyme on silica gel enhances the stability with respect to the effect of pH and oxidizing agent concentrations
addition of poly(ethylene glycol) results in an increase of 57% for interface-bound CPO and 33% for native enzyme
addition of polyethyleneimine results in enhancement of storage stability against H2O2 deactivation, but does not affect the operational stability of the enzyme
glucose enhances the operational stability by two folds, but exhibits no significant effect on storage stability
interface-assembled enzyme shows improved stability as compared to native enzyme, enzyme deactivation as a result of the side effect of H2O2, still limits the overall productivity of the enzyme
immobilization of chloroperoxidase to silica gel in order to increase its stability either in buffer solution or in the presence of the oxidant tert-butyl hydroperoxide. The binding between enzyme and silica gel results in a non-homogeneous enzyme population. Existence of three different enzyme populations. Two populations of the immobilized enzyme show an apparent increase in the stability both to the pH or to the presence of the oxidant
Results 1 - 10 of 23 > >>