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Literature summary for 4.2.1.1 extracted from

  • Peirce, S.; Russo, M.; Perfetto, R.; Capasso, C.; Rossi, M.; Fernandez-Lafuente, R.; Salatino, P.; Marzocchella, A.
    Kinetic characterization of carbonic anhydrase immobilized on magnetic nanoparticles as biocatalyst for CO2 capture (2018), Biochem. Eng. J., 138, 1-11 .
    View publication on PubMed
Search for more literature for 4.2.1.1

Application

Application Comment Organism
environmental protection carbon dioxide absorption into carbonate solutions, promoted by the enzyme carbonic anhydrase, is proposed as potential technology for CO2 capture. The use of solid CA-based biocat-alysts allows the enzyme recovery and reuse under continuous operating conditions typical of industrial applications Caminibacter sp.

Protein Variants

Protein Variants Comment Organism
additional information development and the kinetic characterization of a solid CA-based biocatalyst to be used in CO2 capture processes based on reactive absorption. The commercially availbale technical grade thermostable CA is immobilized by covalent bonding on aminated paramagnetic Fe3O4 nanoparticles via carbodiimide activation of the enzyme. The effective covalent binding of the enzyme on the support is verified in the alkaline carbonate solution used as solvent for CO2 absorption tests. The kinetics of the biocatalyst are assessed by means of CO2 absorption tests in a stirred cell reactor. The liquid solvents used in the CO2 absorption tests are 0.5 M Na2CO3/NaHCO3 buffer, pH 9.6, at 25°C and 40°C and 10% w/w K2CO3 solutions at different carbonate conversion degrees (0-40%). Intrinsic second order kinetic constant kcat/KM for the CO2 hydration reaction catalyzed by the immobilized CA and method validation Caminibacter sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information intrinsic second order kinetic constant kcat/KM for the CO2 hydration reaction catalyzed by the immobilized CA Caminibacter sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required, metalloenzyme Caminibacter sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2CO3 Caminibacter sp.
-
 CO2 + H2O
-
 r

Organism

Organism UniProt Comment Textmining
Caminibacter sp.
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation thermostable enzyme Caminibacter sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2CO3
-
 Caminibacter sp. CO2 + H2O
-
 r