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 | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics at pH 3.0, 20°C | Leptoxyphium fumago |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
RH + chloride + H2O2 | Leptoxyphium fumago | - |
RCl + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leptoxyphium fumago | P04963 | Caldariomyces fumago | - |
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 | Comment | Organism |
---|---|---|
chloroperoxidase | - |
Leptoxyphium fumago |
CPO | - |
Leptoxyphium fumago |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
free enzyme | Leptoxyphium fumago |
42 | 50 | immobilized enzyme | Leptoxyphium fumago |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
3 | - |
assay at | Leptoxyphium fumago |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Leptoxyphium fumago |