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1.11.1.10: chloride peroxidase

This is an abbreviated version!
For detailed information about chloride peroxidase, go to the full flat file.

Word Map on EC 1.11.1.10

Reaction

RH
+
chloride
 +
H2O2
=
RCl
 + 2 H2O

Synonyms

CCPO, Chloride peroxidase, chloroperoxidase, chloroproxidase, CPO, CPO-I, CPO2, haeme-thiolate peroxidase, heme-containing CPO, heme-thiolate chloroperoxidase, More, peroxidase, chloride, Vanadium chloride peroxidase, vCPO

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.10 chloride peroxidase

General Stability

General Stability on EC 1.11.1.10 - chloride peroxidase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
enhanced stability in ionic liquids
-
enzyme immobilized on monoaminoethyl-N-aminoethyl through carbodiimide-coupled method shows an increase in apparent half-life time of more than 500fold that of the soluble enzyme
-
glucose enhances the operational stability by two folds, but exhibits no significant effect on storage stability
-
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
-
immobilization of the enzyme on silica gel enhances the stability with respect to the effect of pH and oxidizing agent concentrations
-
immobilized CPO (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads) retains 83% of its initial activity after 12 cycles of usage
-
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
-
PEG200 and glycerol are the most efficient stabilizer for CPO in temperatures ranging from 25°C to 60°C. Trehalose is more helpful than other sugars for extended storage of CPO
-
stability of the immobilized CPO (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads) is improved compared to free form
-
stability studies on the chloroperoxidase complexes in presence of tert-butyl hydroperoxide
-
the catalytic efficiency of free CPO is decreased about 1.6fold upon immobilization. The conjugated-CPO activity on the poly(hydroxypropyl)methacrylateco-poly(ethylene glycol)-methacrylate-3 membrane remains almost the same as the original activity after 9 cycles. After that, a steady decrease in chlorination capability of the conjugated-CPO is observed, and this loss reaches about 27% after 25 cycles of batch operation
-
the enzyme tolerates up to 30% v/v 1,3-dimethylimidazolium methylsulfate or 1-butyl-3-methylimidazolium methylsulfate
-
the thermostability of peroxidase of CPO is increased about 2fold upon these chemical modification by citraconic anhydride, phthalic anhydride or maleic anhydride. The thermostability of sulfoxidation activity of CPO is increased about 1.2fold upon the chemical modification by citraconic anhydride, phthalic anhydride or maleic anhydride
-