Enzymatic conversion of CO2 to bicarbonate in functionalized mesoporous silica

We report here a concept converting carbon dioxide to biocarbonate in a biomimetic nanoconfiguration. Carbonic anhydrase (CA), the fastest enzyme that can covert carbon dioxide to bicarbonate, can be spontaneously entrapped in carboxylic acid group-functionalized mesoporous silica (HOOC-FMS) with super-high loading density (up to 0.5 mg of protein/mg of FMS) in sharp contrast to normal porous silica. The binding of CA to HOOC-FMS resulted in a partial conformational change comparing to the enzyme free in solution, but it can be overcome with increased protein loading density. The higher the protein loading density, the less conformational change, hence the higher enzymatic activity and the higher enzyme immobilization efficiency (up to >60%). The released enzyme still displayed the native conformational structure and the same high enzymatic activity as that prior to the enzyme entrapment, indicating that the conformational change resulted from the electrostatic interaction of CA with HOOC-FMS was not permanent. This work may provide a new approach converting carbon dioxide to biocarbonate that can be integrated with the other part of biosynthesis process for the assimilation of carbon dioxide.

[1]  Jun Liu,et al.  Probing mechanisms for enzymatic activity enhancement of organophosphorus hydrolase in functionalized mesoporous silica. , 2009, Biochemical and biophysical research communications.

[2]  T. Chakrabarti,et al.  Bio-sequestration of carbon dioxide using carbonic anhydrase enzyme purified from Citrobacter freundii , 2009 .

[3]  Raymond Davy,et al.  Development of catalysts for fast, energy efficient post combustion capture of CO2 into water; an alternative to monoethanolamine (MEA) solvents , 2009 .

[4]  W. Eisenreich,et al.  A dicarboxylate/4-hydroxybutyrate autotrophic carbon assimilation cycle in the hyperthermophilic Archaeum Ignicoccus hospitalis , 2008, Proceedings of the National Academy of Sciences.

[5]  M. Badger,et al.  Advances in understanding the cyanobacterial CO2-concentrating-mechanism (CCM): functional components, Ci transporters, diversity, genetic regulation and prospects for engineering into plants. , 2008, Journal of experimental botany.

[6]  Jun Liu,et al.  Enzyme specific activity in functionalized nanoporous supports , 2008, Nanotechnology.

[7]  G. Fuchs,et al.  A 3-Hydroxypropionate/4-Hydroxybutyrate Autotrophic Carbon Dioxide Assimilation Pathway in Archaea , 2007, Science.

[8]  Jun Liu,et al.  Synergetic effects of nanoporous support and urea on enzyme activity. , 2007, Nano letters.

[9]  Jun Liu,et al.  Characterization of functionalized nanoporous supports for protein confinement , 2006, Nanotechnology.

[10]  G. Whitesides,et al.  Effects of Surface Charge on Denaturation of Bovine Carbonic Anhydrase , 2006, Chembiochem : a European journal of chemical biology.

[11]  Ron Zevenhoven,et al.  Chemical fixation of CO2 in carbonates: Routes to valuable products and long-term storage , 2006 .

[12]  G. M. Bond,et al.  Biomimetic Sequestration of CO2 in Carbonate Form: Role of Produced Waters and Other Brines , 2005 .

[13]  Huan‐Xiang Zhou Protein folding and binding in confined spaces and in crowded solutions , 2004, Journal of molecular recognition : JMR.

[14]  S. Bhattacharya,et al.  CO2 hydration by immobilized carbonic anhydrase , 2003, Biotechnology and applied biochemistry.

[15]  Jun Liu,et al.  Entrapping enzyme in a functionalized nanoporous support. , 2002, Journal of the American Chemical Society.

[16]  B. K. Hodnett,et al.  Mechanistic and Structural Features of Protein Adsorption onto Mesoporous Silicates , 2002 .

[17]  K A Dill,et al.  Stabilization of proteins in confined spaces. , 2001, Biochemistry.

[18]  S. Breton,et al.  The cellular physiology of carbonic anhydrases. , 2001, JOP : Journal of the pancreas.

[19]  A. Minton,et al.  The Influence of Macromolecular Crowding and Macromolecular Confinement on Biochemical Reactions in Physiological Media* , 2001, The Journal of Biological Chemistry.

[20]  P. Wright,et al.  Enzyme immobilisation using siliceous mesoporous molecular sieves , 2001 .

[21]  John Stringer,et al.  Development of Integrated System for Biomimetic CO2 Sequestration Using the Enzyme Carbonic Anhydrase , 2001 .

[22]  T. Kajino,et al.  Catalytic Activity in Organic Solvents and Stability of Immobilized Enzymes Depend on the Pore Size and Surface Characteristics of Mesoporous Silica , 2000 .

[23]  Jun Liu,et al.  Molecular Assembly in Ordered Mesoporosity: A New Class of Highly Functional Nanoscale Materials , 2000 .

[24]  Galen D. Stucky,et al.  MESOPOROUS SILICATE SEQUESTRATION AND RELEASE OF PROTEINS , 1999 .

[25]  M. Aresta,et al.  Enzymatic synthesis of 4-OH-benzoic acid from phenol and CO2: the first example of a biotechnological application of a Carboxylase enzyme , 1998 .

[26]  J. Randerson,et al.  Primary production of the biosphere: integrating terrestrial and oceanic components , 1998, Science.

[27]  Fredrickson,et al.  Triblock copolymer syntheses of mesoporous silica with periodic 50 to 300 angstrom pores , 1998, Science.

[28]  Kenneth M. Kemner,et al.  Functionalized Monolayers on Ordered Mesoporous Supports , 1997 .

[29]  J. Edmonds,et al.  Economic and environmental choices in the stabilization of atmospheric CO2 concentrations , 1996, Nature.

[30]  J. Y. Song,et al.  Thermal, operational, and storage stability of immobilized carbonic anhydrase in membrane lungs. , 1992, ASAIO journal.

[31]  K. Balkus,et al.  Mesoporous molecular sieve immobilized enzymes , 1998 .

[32]  S. Lindskog Structure and mechanism of carbonic anhydrase. , 1997, Pharmacology & therapeutics.