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EC Number
General Stability
Reference
0.3 mM H2O2, 20 h: 58% activity for immobilized enzyme, 43% activity for free enzyme
1.5 M urea, 20 h: 99% activity for immobilized enzyme, 68% activity for free enzyme
15 mM H2O2, 5 min: complete inactivation of free enzyme
30 mM H2O2, 5 min: 80% residual activity for the cross-linked enzyme aggregates
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
covalently bonded CPO on the mesoporous material SBA-15 exhibits a higher operational stability in a continuously operated fixed-bed reactor compared to a catalyst prepared by physisorption of the enzyme. Chloroperoxidase immobilization into SBA-15 shows a remaining activity of about 9%
cross-linked enzyme aggregates exhibit greatly improved stability in the presence of H2O2
crystal crosslinking with glutaraldehyde yields a chloroperoxidase preparation with enhanced thermal resistance compared to soluble enzyme
di(ethylene glycol) and di(propylene glycol) stabilize the enzyme towards denaturation by H2O2
Results 1 - 10 of 23 > >>