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Literature summary for 4.2.1.1 extracted from
- Immobilization and characterization of human carbonic anhydrase I on amine functionalized magnetic nanoparticles (2017), Process Biochem., 57, 95-104 .
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | immobilized hCA I on the magnetic nanoparticles has high operational stability and magnetic recovery which is desirable for biotechnological applications | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | enzyme immobilization on magnetic nanoparticles (MNPs) by co-precipitation method. Silica coating with tetraethyl orthosilicate and amine functionalization of silica coated MNPs by using 3-aminopropyltriethoxysilane are performed. After activation with glutaraldehyde of silica coated MNPs, human carbonic anhydrase (hCA I) is immobilized on silica coated MNPs. Characterization of nanoparticles by transmission electron microscopy, fourier transform infrared spectroscopy, X-ray powder diffraction, and vibrating sample magnetometer. Method evaluation and optimization with respecto to activity, kinetic parameters (Km, Vmax, kcat, kcat/Km), thermal stability, storage stability and reusability of immobilized enzyme, overview. The immobilized hCA I possesses a better thermal stability than free hCA I at 30-50°C. After 40 days storage, the free hCA I sustains 50% and 0.11% of its original activity, whereas the immobilized hCA I retains 89% and 85% of its original activity at 4°C and 25°C, respectively. The immobilized hCA I retains 61% of its initial activity after successively utilization for 13 cycles | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics of free and immobilized enzymes with esterase activity on substrate 4-nitrophenyl acetate | Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required, metalloenzyme | Homo sapiens |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| H2CO3 | Homo sapiens | - |
CO2 + H2O | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P00915 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native isozyme hCA I from human blood erythrocytes by L-tyrosine-p-aminobenzene sulfonamide affinity chromatography | Homo sapiens |
Storage Stability
| Storage Stability | Organism |
|---|---|
| after 40 days storage, the free hCA I sustains 50% and 0.11% of its original activity, whereas the immobilized hCA I retains 89% and 85% of its original activity at 4°C and 25°C, respectively | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| H2CO3 | - |
Homo sapiens | CO2 + H2O | - |
r | |
| additional information | enzyme activity measurement by determining the enzyme's esterase activity with substrate 4-nitrophenyl acetate | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CA1 | - |
Homo sapiens |
| hCA I | - |
Homo sapiens |
| human carbonic anhydrase I | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
immobilized enzyme | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
immobilized enzyme | Homo sapiens |
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