Entrapment of the Fastest Known Carbonic Anhydrase with Biomimetic Silica and Its Application for CO2 Sequestration

Capturing and storing CO2 is of prime importance. The rate of CO2 sequestration is often limited by the hydration of CO2, which can be greatly accelerated by using carbonic anhydrase (CA, EC 4.2.1.1) as a catalyst. In order to improve the stability and reusability of CA, a silica-condensing peptide (R5) was fused with the fastest known CA from Sulfurihydrogenibium azorense (SazCA) to form R5-SazCA; the fusion protein successfully performed in vitro silicification. The entrapment efficiency reached 100% and the silicified form (R5-SazCA-SP) showed a high activity recovery of 91%. The residual activity of R5-SazCA-SP was two-fold higher than that of the free form when stored at 25 °C for 35 days; R5-SazCA-SP still retained 86% of its activity after 10 cycles of reuse. Comparing with an uncatalyzed reaction, the time required for the onset of CaCO3 formation was shortened by 43% and 33% with the addition of R5-SazCA and R5-SazCA-SP, respectively. R5-SazCA-SP shows great potential as a robust and efficient biocatalyst for CO2 sequestration because of its high activity, high stability, and reusability.

[1]  Dong Wook Lee,et al.  High-level production in a plant system of a thermostable carbonic anhydrase and its immobilization on microcrystalline cellulose beads for CO2 capture , 2020, Plant Cell Reports.

[2]  I. Ng,et al.  ARduino‐pH Tracker and screening platform for characterization of recombinant carbonic anhydrase in Escherichia coli , 2019, Biotechnology progress.

[3]  M. Yoshimoto,et al.  Immobilized carbonic anhydrase: preparation, characteristics and biotechnological applications , 2018, World Journal of Microbiology and Biotechnology.

[4]  T. Satyanarayana,et al.  Microbial Carbonic Anhydrases in Biomimetic Carbon Sequestration for Mitigating Global Warming: Prospects and Perspectives , 2017, Front. Microbiol..

[5]  M. Bonn,et al.  The Structure of the Diatom Silaffin Peptide R5 within Freestanding Two-Dimensional Biosilica Sheets. , 2017, Angewandte Chemie.

[6]  K. D'Ambrosio,et al.  Thermostable Carbonic Anhydrases in Biotechnological Applications , 2015, International journal of molecular sciences.

[7]  C. Supuran,et al.  Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense. , 2015, Bioorganic & medicinal chemistry letters.

[8]  P. Booth,et al.  Structure and function of the silicifying peptide R5. , 2015, Journal of materials chemistry. B.

[9]  Byung Hoon Jo,et al.  Bioinspired Silica Nanocomposite with Autoencapsulated Carbonic Anhydrase as a Robust Biocatalyst for CO2 Sequestration , 2014 .

[10]  L. Chien,et al.  Biosequestration of carbon dioxide using a silicified carbonic anhydrase catalyst , 2013, Biotechnology and Bioprocess Engineering.

[11]  Siddharth V. Patwardhan,et al.  CO2 sequestration by enzyme immobilized onto bioinspired silica. , 2013, Chemical communications.

[12]  C. Supuran,et al.  An α-carbonic anhydrase from the thermophilic bacterium Sulphurihydrogenibium azorense is the fastest enzyme known for the CO2 hydration reaction. , 2013, Bioorganic & medicinal chemistry.

[13]  C. Supuran,et al.  Anion inhibition studies of the fastest carbonic anhydrase (CA) known, the extremo-CA from the bacterium Sulfurihydrogenibium azorense. , 2012, Bioorganic & medicinal chemistry letters.

[14]  M. Rossi,et al.  Biochemical properties of a novel and highly thermostable bacterial α-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1 , 2012, Journal of enzyme inhibition and medicinal chemistry.

[15]  B. Smit,et al.  Carbon dioxide capture: prospects for new materials. , 2010, Angewandte Chemie.

[16]  L. Betancor,et al.  Bioinspired enzyme encapsulation for biocatalysis. , 2008, Trends in biotechnology.

[17]  Cheng-Kang Lee,et al.  Biosilicification of dual‐fusion enzyme immobilized on magnetic nanoparticle , 2008, Biotechnology and bioengineering.

[18]  Pingping Li,et al.  Impact of Zn, Cu, and Fe on the Activity of Carbonic Anhydrase of Erythrocytes in Ducks , 2007, Biological Trace Element Research.

[19]  N. Kröger,et al.  Silica formation in diatoms: the function of long-chain polyamines and silaffins , 2004 .

[20]  Rajesh R Naik,et al.  Enzyme immobilization in a biomimetic silica support , 2004, Nature Biotechnology.

[21]  Marc R. Knecht,et al.  Functional analysis of the biomimetic silica precipitating activity of the R5 peptide from Cylindrotheca fusiformis. , 2003, Chemical communications.

[22]  Kerry S. Smith,et al.  Prokaryotic carbonic anhydrases. , 2000, FEMS microbiology reviews.

[23]  W. Dreybrodt,et al.  The kinetics of the reaction CO2 + H2O → H+ + HCO3− as one of the rate limiting steps for the dissolution of calcite in the system H2OCO2CaCO3 , 1996 .

[24]  Crippa Monica,et al.  Fossil CO2 emissions of all world countries - 2020 Report , 2020 .