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Literature summary for 1.11.1.10 extracted from

  • Gao, F.; Guo, Y.; Fan, X.; Hu, M.; Li, S.; Zhai, Q.; Jiang, Y.; Wang, X.
    Enhancing the catalytic performance of chloroperoxidase by co-immobilization with glucose oxidase on magnetic graphene oxide (2019), Biochem. Eng. J., 143, 101-109 .
No PubMed abstract available
Search for more literature for 1.11.1.10

Application

Application Comment Organism
synthesis chloroperoxidase (CPO) has long been recognized as a powerful and versatile catalyst, potential of co-immobilized enzymes chloroperoxidase and glucose oxidase as MGO-GOx-CPO in environmental applications Leptoxyphium fumago

Protein Variants

Protein Variants Comment Organism
additional information enhancement of the catalytic performance of chloroperoxidase by co-immobilization with glucose oxidase (GOx) on magnetic graphene oxide (MGO), the catalytic efficiency (kcat/Km) of CPO immobilized on either MGO or MGO-GOx is approximately 2.1 and 2.5times higher, respectively, compared to that of the free CPO. The superior catalytic enzymes chloroperoxidase and glucose oxidase are co-immobilized onto the surface of MGO, method development and evaluation, overview. Graphene oxide/iron oxide (MGO) composites functionalized with Fe3O4 nanoparticles, providing the magnetic property, are used. The magnetism of the composites allows easy separation of the enzyme for reuse while the unique surface property of the composites significantly enhances the catalytic performance of the enzyme. The catalytic efficiency of immobilized CPO is much higher than that of free CPO. Immobilized CPO can be effectively and conveniently recovered and is ready to reuse. Enzyme cascade helps to harness the power of enzymes requiring auxiliary proteins. MGO-GOx-CPO reaches its peak activity (95.2%) when temperature is maintained between 42°C and 50°C compared to the optimal temperature of 35°C for the free enzyme. MGO-GOx-CPO reuse shows a good recovery in the presence of an external magnetic field, with about 38.5% activity remaining after 6 cycles of applications Leptoxyphium fumago

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics at pH 3.0, 20°C Leptoxyphium fumago

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
RH + chloride + H2O2 Leptoxyphium fumago
-
 RCl + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago P04963 Caldariomyces fumago
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information CPO-catalyzed degradation of the dyes Orange G, acid blue 45, or crystal violet from wastewater samples, kinetics at pH 3.0, 20°C Leptoxyphium fumago ?
-
-
RH + chloride + H2O2
-
 Leptoxyphium fumago RCl + 2 H2O
-
 ?

Synonyms

Synonyms Comment Organism
chloroperoxidase
-
 Leptoxyphium fumago
CPO
-
 Leptoxyphium fumago

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 free enzyme Leptoxyphium fumago
42 50 immobilized enzyme Leptoxyphium fumago

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 70 the immobilized CPO retains more than 60% of its initial activity after 10 h incubation at 50ºC, while free CPO completely loses its activity. At 70°C, free CPO keeps only about 10% of its initial activity, while immobilized MGO-CPO retains approximately 30% of initial activity after 1 h Leptoxyphium fumago

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
-
 assay at Leptoxyphium fumago

Cofactor

Cofactor Comment Organism Structure
heme
-
 Leptoxyphium fumago