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Literature summary for 4.2.1.1 extracted from
- Expression and characterization of a codon-optimized alkaline-stable carbonic anhydrase from Aliivibrio salmonicida for CO2 sequestration applications (2017), Bioprocess Biosyst. Eng., 40, 413-421 .
Application
| Application | Comment | Organism |
|---|---|---|
| environmental protection | recombinant engineered mASCA enzyme exhibits high production yield and sufficient stabilities against relatively high temperature and alkaline pH, which are required conditions for the development of more efficient enzymatic CCS systems. Carbon capture and storage (CCS) is a technology that can capture up to 90% of the carbon dioxide (CO2) emissions produced from the use of fossil fuels in electricity generation and industrial processes, preventing the carbon dioxide from entering the atmosphere. mASCA has the potential to play an important role in CCS systems, particularly in an enzyme-based CO2 capture system that requires large amounts of CA enzyme | Aliivibrio salmonicida |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Aliivibrio salmonicida |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | design of a mature form ofASCA(mASCA) using a codon optimization of ASCA gene and removal of the ASCA signal peptide. mASCA is highly expressed and highly stable. The recombinant engineered enzyme ASCA can promote CO2 absorption in an alkaline solvent required for efficient carbon capture | Aliivibrio salmonicida |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| acetazolamide | about 70% inhibition at 1 mM | Aliivibrio salmonicida |  |
| azide | about 30% inhibition at 1 mM | Aliivibrio salmonicida | |
| Iodide | about 30% inhibition at 1 mM | Aliivibrio salmonicida | |
| nitrate | about 70% inhibition at 1 mM | Aliivibrio salmonicida | |
| sulfanilamide | about 70% inhibition at 1 mM | Aliivibrio salmonicida | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required | Aliivibrio salmonicida | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| H2CO3 | Aliivibrio salmonicida | - |
CO2 + H2O | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aliivibrio salmonicida | B6EIU7 | i.e. Vibrio salmonicida strain LFI1238 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Aliivibrio salmonicida |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| H2CO3 | - |
Aliivibrio salmonicida | CO2 + H2O | - |
r | |
| additional information | recombinant engineered enzyme ASCA exhibits esterase activity with 4-nitrophenyl acetate and can promote CO2 absorption in an alkaline solvent required for efficient carbon capture. Recombinant mASCA is capable of catalyzing the conversion of CO2 to CaCO3 (calcite form) in the presence of Ca2+. The CO2 hydration activity is determined by monitoring the time required for the pH of the assay solution to change from 8.3 to 7.0 and using the formula [[(t0 - tc)/tc]/protein(mg)] [Wilbur-Anderson units (WAU) per mg of protein] | Aliivibrio salmonicida | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 26000, about, recombinant optimized enzyme without signal peptide, SDS-PAGE, x * 25715, sequence calculation | Aliivibrio salmonicida |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alpha-type CA | - |
Aliivibrio salmonicida |
| ASCA | - |
Aliivibrio salmonicida |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
CO2 hydration assay at room temperature | Aliivibrio salmonicida |
| 25 | - |
esterase activity assay at, p-NPA hydrolysis | Aliivibrio salmonicida |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 60 | activity range, esterase activity of recombinant enzyme | Aliivibrio salmonicida |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
purified recombinant enzyme mASCA, retains over 90% activity after 15 min | Aliivibrio salmonicida |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Aliivibrio salmonicida |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 11 | activity range, esterase activity of recombinant enzyme | Aliivibrio salmonicida |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | - |
purified recombinant enzyme mASCA, about 30% activity remaining after 15 min | Aliivibrio salmonicida |
| 5 | - |
purified recombinant enzyme mASCA, about 70% activity remaining after 15 min | Aliivibrio salmonicida |
| 6 | 11 | purified recombinant enzyme mASCA, over 90% activity remaining after 15 min within this range | Aliivibrio salmonicida |
| 10 | - |
purified recombinant enzyme mASCA, over 90% activity remaining after 48 h, 70% after 72 h | Aliivibrio salmonicida |
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