1.11.1.10	0.3 mM H2O2, 20 h: 58% activity for immobilized enzyme, 43% activity for free enzyme	696905	
1.11.1.10	1.5 M urea, 20 h: 99% activity for immobilized enzyme, 68% activity for free enzyme	696905	
1.11.1.10	15 mM H2O2, 5 min: complete inactivation of free enzyme	695425	
1.11.1.10	30 mM H2O2, 5 min: 80% residual activity for the cross-linked enzyme aggregates	695425	
1.11.1.10	addition of poly(ethylene glycol) results in an increase of 57% for interface-bound CPO and 33% for native enzyme	674983	
1.11.1.10	addition of polyethyleneimine results in enhancement of storage stability against H2O2 deactivation, but does not affect the operational stability of the enzyme	674983	
1.11.1.10	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%	712193	
1.11.1.10	cross-linked enzyme aggregates exhibit greatly improved stability in the presence of H2O2	699598	
1.11.1.10	crystal crosslinking with glutaraldehyde yields a chloroperoxidase preparation with enhanced thermal resistance compared to soluble enzyme	657725	
1.11.1.10	di(ethylene glycol) and di(propylene glycol) stabilize the enzyme towards denaturation by H2O2	658334