Available online at www.sciencedirect.
com
Biotechnology for the acceleration of carbon dioxide
capture and sequestration
Christopher K Savile and James J Lalonde
The potential for enzymatic acceleration of carbon dioxide
capture from combustion products of fossil fuels has been
demonstrated. Carbonic anhydrase (CA) accelerates post
combustion CO2 capture, but available CAs are woefully
inadequate for the harsh conditions employed in most of these
processes. In this review, we summarize recent approaches to
improve CA, and processes employing this enzyme, to maximize
the benefit from this extremely fast biocatalyst. Approaches to
overcoming limitations include sourcing CAs from thermophilic
organisms, using protein engineering to evolve thermo-tolerant
enzymes, immobilizing the enzyme for stabilization and
confinement to cooler regions and process modifications that
minimize the (thermo-, solvent) stress on the enzyme.
Address
Codexis, Incorporated, 200 Penobscot Drive, Redwood City, CA 94063,
USA
Corresponding author: Lalonde, James J (james.lalonde@codexis.com)
Current Opinion in Biotechnology 2011, 22:818823
This review comes from a themed issue on
Chemical biotechnology
Edited by Guo-Qiang Chen and Romas Kazlauskas
Available online 5th July 2011
0958-1669/$ see front matter
Published by Elsevier Ltd.
DOI 10.1016/j.copbio.2011.06.006
Introduction
Carbonic anhydrase (CA, E.C. 4.2.1.1) is among the fastest
known enzymes, catalyzing the hydration of CO2 into
bicarbonate and a proton at turnover numbers approaching
106/s (reaction (1)). The enzyme is ubiquitous in Nature
(mammals, plants, algae and bacteria), and is an archetypal
example of convergent evolution [1], with at least five
distinct classes: a, b, g, d and z which bear little structural
similarity, but all employ an active site divalent zinc ion or
related metal for catalysis (Figure 1) [2], Central to the
hydration mechanism is the nucleophilic attack of a Zn(II)
bound hydroxide on CO2 [3], Recently CA enzymes have
been identified as having potential to accelerate CO2
capture from large combustion emitters [4]:
CO2 H2 O HCO3  H (1) enzyme (for both stabilization and restriction to the cooler
Overwhelming evidence has shown that CO2 emission
from the combustion of fossil fuels is a major contributor
to global climate change with potentially devastating
Current Opinion in Biotechnology 2011, 22:818823
effects. While energy production technologies exist to
limit or even eliminate carbon dioxide emission, fully half
of the electricity in the United States is generated from
the combustion of cheap and abundant coal, and coal
combustion is responsible for 40% of fossil fuel derived
CO2 emissions worldwide.
Thus, CO2 capture and sequestration (CCS) has been
identified as the critical enabling technology to reduce
CO2 emissions significantly, while allowing the continued
use of coal [6]. The position of equilibrium of reaction (1)
is far to the left, so CCS processes employing CA, must do
so in either an alkaline capture solvent approach (e.g.
aqueous monoethanolamine (MEA), potassium carbonate
or methyldiethanolamine (MDEA)) to neutralize the
proton released or must use a biomineralization approach
in which high levels of divalent calcium or magnesium
precipitate CO2 as solid carbonate.
Use of CA in solvent-based PCCC
Chemical absorption with regenerable alkaline aqueous
solvents is considered the nearest term option for post
combustion CCS [7]. In this process (Figure 2), CO2 is
removed from the flue gas stream in the absorber column
and then desorbed in a heated stripper column to give
relatively pure CO2 for compression and storage. The
challenge facing these capture processes is in energy loss
in desorption. Solvents such as MEA tend to bind CO2
tightly such that the parasitic energy loss in desorbing the
CO2 would result in a near doubling of the cost of
electricity [8].
CA has been shown to facilitate the use of aqueous
solvents with a far lower heat of desorption (e.g. hindered
and tertiary amines), thus enabling a far lower energy
penalty on CCS [9]. Absorption of CO2 tends to be
slower in these solvents and thus requires the use of an
accelerant such as CA. The poor stability and activity of
naturally derived CA under the harsh conditions of these
processes i.e. temperatures from 50 to over 1258C, high
concentrations of organic amine, trace contaminants such
as heavy metals, and sulfur and nitrogen oxides, have
limited their use. Approaches to overcoming these limita-
tions have included sourcing CAs from thermophilic
organisms, using protein engineering techniques to create
thermo-tolerant enzymes [10,11], immobilizing the
process zones) or process modifications such as cooling of
the flue gas. Small molecule analogs of CA have been
reported with potentially higher stability than proteins,
www.sciencedirect.com
 Biotechnology for CO2 capture and sequestration Savile and Lalonde 819

Figure 1

(a) (b) (c) (d)

Current Opinion in Biotechnology

Depiction of the X-ray crystal structures of four carbonic anhydrases from different families [5]. (a) Type II a-class carbonic anhydrase from Homo
sapiens (1ca2.pdb). (b) The tetrameric form of the b-class carbonic anhydrase from Mycobacterium tuberculosis (2a5v.pdb). (c) The trimeric form of a
g-class carbonic anhydrase from Thermosynechococcus elongatus (3kwc.pdb). (d) The z-class carbonic anhydrase from Thalassiosira weissflogii
(3bob.pcb). A crystal structure of a d-class CA has not been reported.

Figure 2

Scrubbed
Pure CO2 (>90%) for
Flue Gas Compression and
Storage
Lean Solvent

CO2 CO2
Absorber Stripper
Column Column
Enzyme Enzyme

Rich Solvent
Steam
Flue Gas
with CO2

40-60C Higher Heat

Current Opinion in Biotechnology

Solvent-based PCCC schematic.

but their rates of acceleration tend to be orders of mag-
nitude less than the enzymes [12,13,14,15]. Very
recently, however, a Ni(II) complex has been reported
with rates within an order of magnitude of the fastest CAs,
albeit in nonaqueous media [16].
Because of the economic impact of the problem and the
multiple industrial applications, the field is dominated by
patents rather than publications in the open scientific
literature. CO2 Solution (Quebec, Canada) has a patent
portfolio on the use of CAs for CO2 capture from combus-
tions sources. Besides covering carbon capture from fossil
fuel combustion [17], they describe the use of CA to
accelerate capture in solvents such as MEA, MDEA, and
piperazine [18]. The conditions described are at near
ambient temperatures and dilute aqueous solvents, pre-
sumably due to the sensitivity of the human enzyme.
Generally, these CA accelerated capture processes
employ immobilized CA in contact with CO2. CO2
Solution describes the use of CA in various bioreactor
formats including a packed column [9] triphasic bubble
reactor, a tower reactor and a spray absorber [19]. Others
have described process formats for capture of CO2 from
combustion sources using CAs entrapped in a gas per-
meable membrane [2022].Thermostable CAs for sol-
vent-based PCCC

www.sciencedirect.com Current Opinion in Biotechnology 2011, 22:818823

820 Chemical biotechnology
Given the high temperature for regeneration in a solvent-
based capture system, thermophilic organisms represent a
source of stable CAs. Three CAs from thermophilic
organisms have been the primary focus of most bio-
chemical studies. A g-class CA from Methanosarcina ther-
mophila (CAM) [23], a b-class CA from Methanobacterium
thermoautotrophicum (CAB) [24] and a g-class CA from
Pyrococcus horikoshii [25]. CAM shows optimal activity at
558C, with kcat values approaching 105/s. CAM is a rela-
tively stable CA it shows 50% residual activity after
15 min at 708C and is inactivated at 758C [26]. CAB shows
optimal activity at 708C. It is more thermostable than
CAM, showing 50% residual activity after 15 min at
858C and inactivation at 908C, but has a lower kcat value
of 104/s [27]. The activity of CA from P. horikoshii has not
been fully characterized, but its host organism shows
optimal growth at 988C [23]. By comparison, Human
CA II shows optimal activity at 378C and is inactivated
above 508C [26]. However, it is an extremely fast enzyme
with a kcat of 106/s [27].
Several heat-stable CAs for extraction of CO2 from CO2-
containing media have been reported [28,29]. An a-
class CA from Bacillus clausii showed higher thermostabil-
ity than CAM with 17% residual activity (via the Wilbur-
Andersen assay) after 15 min at 808C in 1 M sodium
bicarbonate pH 8.05. At 0.6 g/L enzyme loading, this
CA could extract >99% of CO2 from a 15% CO2 gas
stream versus only 33% removal without CA. The CA also
increased the CO2 extracted with MEA solutions by
twofold, albeit at the low MEA concentration of 1%.
CA from the thermophilic organism Caminibacter media-
tlanticus DSM 16658 had a melting temperature of 1098C
at pH 9 and retained 40% of its original activity after
15 min in 1 M sodium bicarbonate at 1008C, and also
increased the amount of CO2 extracted with 1 M sodium
bicarbonate pH 9 solutions [30]. While thermophiles
represent a good source of thermostable CAs, naturally
occurring CAs typically do not show suitable activity or
Figure 3
1000000 75C (24 h), 15X
100000 65C (24 h), 10X
Compounded Fold
Improvement
10000 53C (24 h), 40X
1000
50C (24 h), 70X
100
10
1 0
1 2 3 4
Evolution Round
(a) Directed evolution of CA for increased stability to MDEA. (b) Stability of the round 4 CA evolvant at 758C in 4.2 M MDEA.
Current Opinion in Biotechnology 2011, 22:818823
stability in the presence of high concentrations of alkaline
capture solvents at high temperatures. To our knowledge,
there are no reports in the literature of CA activity or
stability in amine-based captures solvent such as MDEA
or AMP at process relevant concentrations (e.g. 50%, v/v)
and temperatures (>458C).
A better approach might be to engineer, or evolve, a CA
for activity and stability under the nonnatural process
conditions it is expected to operate. The goal would be to
generate a soluble CA biocatalyst capable of catalyzing
CO2 hydration in capture solvents at absorber tempera-
tures (45608C) and, in an ideal case, surviving the high
desorber temperatures (>1008C). Codexis is applying
directed evolution technology to increase the activity
and stability of CAs by screening a wide range of geneti-
cally diverse biocatalysts using high through-put (HTP)
screens that closely mimic solvent-based PCCC process
conditions in MDEA and other amine solvents. Initial
evaluation of 50 wild-type CAs identified a CA from a
mesophilic organism with higher activity and stability in
MDEA than human CAII. It was inactivated at tempera-
tures above 408C in MDEA, but after four rounds of
directed evolution, the temperature of half-inactivation
was increased by >40828C in 5 M MDEA pH 11.8 and
the half-life (t1/2) was increased by ca. five orders of
magnitude to 20 hours in 4.2 M MDEA at 758C
(Figure 3) [31]. Strain engineering of an industrial
enzyme production host for a high titer fermentation
process will allow large-scale production of the biocatalyst
at low cost in order to meet the predicted volumes.
Immobilization of CA
Immobilization of CA is the most common method to
both stabilize the enzyme and to limit exposure to dena-
turing conditions in CCS processes. Immobilization has
been reported on a number of solid supports including
polyamide [32], n-vinyl formamide [33], chitosan [34],
and alkyl sepharose [35].
100
%Residual Activity
80 Rd 3 hit
60
Rd 4 hit
40
20
0 12 24 36 48
Time (h)
Current Opinion in Biotechnology
www.sciencedirect.com
 Biotechnology for CO2 capture and sequestration Savile and Lalonde 821
One strategy to limit the activity loss on immobilization
has been to immobilize in high volume swellable gels
[36,37], foams [38] or to stabilize as soluble polymer
protein conjugates [39]. Alternatively, high surface/
volume ratio materials such as microparticles and nano-
particles [40,41] have been used. Interestingly, simple
acetylation of a CA was shown by Whitesides to increase
kinetic resistance to denaturation, presumably by altering
the surface charge [42].
The activity lost on immobilization of CA can be sub-
stantial; however, this effect is often obscured in most
studies by the use of surrogate assays. Characterization of
immobilized CA has typically been done using p-nitro-
phenyl ester hydrolysis. While convenient, this esterase
assay is only suitable for the a-class CAs. This solution
phase assay does not measure the impact on gasliquid
solid contact [43] and diffusional limitations created by
entrapping the enzyme in a solid form. True gasliquid
activity determinations using a wetted-wall column (JT
Cullinane, Thermodynamics and kinetics of aqueous
piperazine with potassium carbonate for carbon dioxide
absorption, Dissertation, Austin, TX: The University of
Texas at Austin, 2005) or a stirred cell reactor (SCR) [44]
are much better measures of the enzyme performance
under carbon capture process conditions. Evaluation of
immobilization on nylon microparticles or as a cross-
linked enzyme aggregate (CLEA) using gaseous CO2
in a packed column or hydration cell showed that a
smaller particle size favors a higher level of gas/liquid/
solid contact [45].
Membrane-based CO2 extraction with CAs
Biomimetic membrane-based technology has been
employed for extracting CO2. Researchers from the com-
pany carbozymes have described a CA permeator that
consists of two hollow fiber microporous membranes
separated by a thin liquid membrane [46]. The CA is
immobilized on the hollow fiber wall to maximize contact
with CO2 at the gasliquid interface and facilitate CO2
uptake into the liquid membrane by rapid conversion to
bicarbonate, and can enhance the rate of both absorption
and desorption. This technology is applicable for mod-
Table 1
Strategies to overcome stability limitations of carbonic anhydrase under PCCC conditions.
Strategy Potential benefits
Sourcing CAs from thermophiles - High thermostability
Protein engineering - High activity
- High stability
Immobilizing CA for stabilization/ - Longer CA lifetime
confinement to cooler regions
Membrane systems that minimize - CA operates at
stress on CA ambient conditions
www.sciencedirect.com
erate temperature (10858C) [47] gas flows at low to high
pressure with CO2 concentrations from <1% to >20%. In
a related study, entrapment of the enzyme in a contained
liquid membrane phase showed good preservation of
activity [48]. The design may provide cost and perform-
ance advantages over amine scrubbing systems, but there
appear to be some serious drawbacks. These membrane
systems employ a vacuum force on the permeate side of
the membrane to drive diffusion which adds operational
cost and added CO2 compression costs versus solvent
desorption methods. In addition, the permeator is unable
to tolerate heavy metals such as mercury and only able to
tolerate 7 ppmv SOx, while the typical SOx concentrations
in flue gas is >300 ppmv. Thus, heavy metals and SOx
must be reduced by a pretreatment. Even with pretreat-
ment, however, membranes are sensitive to particulates
and may require exchange or cleanup to limit fouling.
Use of CA in biomineralization
CA is part of the biomineralization process in the for-
mation of the exoskeleton of mollusks. This biological
process has been used as a model for CO2 fixation in the
form of carbonate salts of divalent metals. Lee has
recently reviewed the use of CA for CCS and biominer-
alization [49]. Very recently, a strategy introducing the
use of CA to accelerate in bioweathering of silicates was
reported in which CA is used to accelerate to hydration of
CO2 and subsequent precipitation of Mg(II) released
from weathering of magnesium silicate rock [50].
Concluding remarks
The potential for acceleration of carbon dioxide capture
from combustion products of fossil fuels has been clearly
demonstrated. A summary of these approaches is given in
Table 1. Early work using readily available CAs from
mammalian sources has now largely been replaced by
more stable forms derived from thermophiles or directed
evolution approaches. These approaches impressively
illustrate the potential of CA to accelerate CO2 capture
under relevant process conditions. For real progress to
continue, however, careful attention should be paid to the
use of relevant metrics such as direct gas absorption
Potential drawbacks References
- Thermostable b-class and g-class CAs show slower [2327,28,29,30]
rates than mesophilic a-class CAs
- Poor activity in solvent and/or lower temperatures
- CAs may not be evolvable for extreme temperatures [11,31]
- No desorption benefit [9,3241,42]
- Slower rates
- Fouling [4648]
- High energy penalty
Current Opinion in Biotechnology 2011, 22:818823
822 Chemical biotechnology
activity and volumetric activity measurements made
under targeted temperatures and solvent concentrations.
Disclosure
Codexis, Inc. has a Joint Development Agreement with
CO2 Solution, Inc. and is participating in a program with
CO2 Solution for the development of stable forms of
carbonic anhydrase for CO2 capture from coal-fired power
generation plants.
Acknowledgements
The Codexis program was funded in part by the Advanced Research
Projects Agency Energy (ARPA-E), an agency of the United States
Department of Energy, under Award Number DE-AR0000071. We thank
ARPA-E program managers Mark Hartney and Daniel Matuszak for helpful
input and discussions. Oscar Alvizo is acknowledged for the preparation of
Figure 1. CO2 Solution is acknowledged for collaboration and helpful
discussions, and for the use of Figure 2.
References and recommended reading
Papers of particular interest, published within the period of review,
have been highlighted as:
 of special interest
 of outstanding interest
1. Tashian RE: The carbonic anhydrases: widening perspectives
on their evolution, expression and function. BioEssays 1989,
10:186-192.
2. Tripp BC, Smith K, Ferry JG: Carbonic anhydrase: new insights
 for an ancient enzyme. J Biol Chem 2001, 276:48615-48618.
A well-written mini-review describing the structure and catalysis of a, b
and g forms.
3. Silverman DN, Lindskog S: The catalytic mechanism of carbonic
anhydrase: implications of a rate-limiting protolysis of water.
Acc Chem Res 1988, 21:30-36.
4. Chu S: Carbon capture and sequestration. Science 2009,
325:1599.
5. Berman H, Henrick K, Nakamura H: Announcing the worldwide
Protein Data Bank. Nat Struct Biol 2003, 10:98 www.wwpdb.org.
6. Katzer J: The Future of Coal, Options for a Carbon Constrained
World. Cambridge, MA: Massachusetts Institute of Technology;
2007:. 192.
7. Rochelle GT: Amine scrubbing for CO2 capture. Science 2009,
325:1652-1654.
8. Ciferno J, Fout T, Jones A, Murphy JT: Capturing carbon from
existing coal-fired plants. Chem Eng Prog 2009, 105:33-41.
9. Blais R, Rogers P: Process and apparatus for the treatment
 of carbon dioxide with carbonic anhydrase. US Patent
6524843; 2003.
Early report of the use of immobilized CA in a packed tower reactor for
CO2 capture.
10. Newman LM, Clark L, Ching C, Zimmerman S: Carbonic
anhydrase polypeptides and uses thereof. US Patent
WO10081007; 2010.
11. Daigle R, Desrochers M: Carbonic anhydrase having increased
stability under high temperature conditions. US Patent
7521217; 2009.
12. Looney A, Han R, McNeill K, Parkin G:
Tris(pyrazoly1)hydroboratozinc hydroxide complexes as
functional models for carbonic anhydrase: on the nature of the
bicarbonate intermediate. J Am Chem Soc 1993, 115:4690-4697.
13. Parkin G: Synthetic analogues relevant to the structure and
 function of zinc enzymes. Chem Rev 2004, 104:699-768.
A good overview of the advancements in the development of enzyme
mimetics.
Current Opinion in Biotechnology 2011, 22:818823
14. Bergquist C, Fillebeen T, Morlok MM, Parkin G: Protonation and
reactivity towards carbon dioxide of the mononuclear
tetrahedral zinc and cobalt hydroxide complexes,
[TpBut,Me]ZnOH and [TpBut,Me]CoOH: comparison of the
reactivity of the metal hydroxide function in synthetic
analogues of carbonic anhydrase. J Am Chem Soc 2003,
125:6189-6199.
15. Davy R: Development of catalysts for fast, energy efficient post
combustion capture of CO2 into water; an alternative to
monoethanolamine (MEA) solvents. Energy Procedia 2009,
1:885-892.
16. Huang D, Makhlynets OV, Tan LL, Lee SC, Rybak-Akimova EV,
Holm RH: Kinetics and mechanistic analysis of an extremely
rapid carbon dioxide fixation reaction. Proc Natl Acad Sci U S A
2011, 108:1222-1227.
17. Fradette S, Ruel J: Process and a plant for recycling
 carbon dioxide emissions from power plants. US Patent
7596952; 2009.
Patent claims the use of carbonic anhydrases for CO2 capture from fossil
fuel derived power generation.
18. Fradette S, Ceperkovic O: CO2 absorption solution. US Patent
US07699910; 2010.
19. Fradette S: Process and apparatus using a spray absorber
bioreactor for the biocatalytic treatment of gases. US Patent
WO04056455; 2004.
20. Saunders P, Salmon S, Borchert M: Modular reactor
and process for carbon dioxide extraction. US Patent
WO10014773; 2010.
21. Trachtenberg MC: Enzyme systems for gas processing. US
Patent US6143556; 2000.
22. Dziedzic D, Gross KB, Gorski RA, Johnson JT: Sequestration of
carbon dioxide. US Patent US7132090; 2006.
23. Ferry JG: The g class of carbonic anhydrases. Biochim Biophys
Acta (BBA): Proteins Proteomics 2010, 1804:374-381.
24. Rowlett RS: Structure and catalytic mechanism of the b-
carbonic anhydrases. Biochim Biophys Acta (BBA): Proteins
Proteomics 2010, 1804:362-373.
25. Jeyakanthan J, Rangarajan S, Mridula P, Kanaujia SP, Shiro Y,
Kuramitsu SSY, Sekar K: Observation of a calcium-binding
site in the [gamma]-class carbonic anhydrase from
Pyrococcus horikoshii. Acta Crystallogr D Biol Crystallogr 2008,
D64:1012-1019.
26. Alber BE, Ferry JG: Characterization of heterologously
produced carbonic anhydrase from Methanosarcina
thermophila. J Bacteriol 1996, 178:3270-3274.
27. Smith KS, Ferry JG: A plant-type (b-class) carbonic anhydrase
in the thermophilic methanoarchaeon Methanobacterium
thermoautotrophicum. J Bacteriol 1999, 181:6247-6253.
28. Borchert M, Saunders P: Heat-stable carbonic anhydrases and
 their use. US Patent US7803575; 2010.
One of a family of patents from Novozymes reporting on stable CAs from
extremophiles. The enzyme identified in this patent is a highly thermo-
stable carbonic anhydrase from Caminibacter mediatlanticus DSM
16658.
29. Borchert M, Saunders P: Heat stable carbonic anhydrases and
their use. US Patent US7892814; 2011.
30. Borchert M, Saunders P: Heat-stable carbonic anhydrases and
their use. US Patent WO/2010/151787; 2010.
31. Savile C, Nguyen L, Alvizo O, Balatskaya S, Choi G, Benoit M,
 Fusman I, Geilhufe J, Ghose S, Gitin S et al.: Low cost biocatalyst
for the acceleration for energy efficient CO2 capture. 2011
ARPA-E Energy Innovation Summit. Washington, DC: ARPA;
2011.
Report on improving carbonic anhydrase stability by 5 orders of magni-
tude using directed evolution.
32. Belzil A, Parent C: Qualification methods of chemical
immobilizations of an enzyme on solid support. Methodes de
qualification des immobilisations chimiques dune enzyme sur un
support solide 2005, 83:70-77.
www.sciencedirect.com
 Biotechnology for CO2 capture and sequestration Savile and Lalonde 823
33. Drevon GF, Urbanke C, Russell AJ: Enzyme-containing Michael-
adduct-based coatings. Biomacromolecules 2003, 4:675-682.
34. Sharma A, Bhattacharya A, Shrivastava A: Biomimetic CO2
sequestration using purified carbonic anhydrase
from indigenous bacterial strains immobilized on
biopolymeric materials. Enzyme Microb Technol 2011,
48:416-426.
35. Azari F, Nemat-Gorgani M: Reversible denaturation of carbonic
anhydrase provides a method for its adsorptive
immobilization. Biotechnol Bioeng 1999, 62:193-199.
36. Ray B: Purification and immobilization of human carbonic
anhydrase B by using polyacrylamide gel. Experientia 1977,
33:1439-1440.
37. Zhang YT, Fan LH, Zhi TT, Zhang L, Huang H, Chen HL: Synthesis
and characterization of poly(acrylic acid-co-acrylamide)/
hydrotalcite nanocomposite hydrogels for carbonic
anhydrase immobilization. J Polym Sci A Polym Chem 2009,
47:3232-3240.
38. Ozdemir E: Biomimetic CO2 sequestration. 1. Immobilization of
carbonic anhydrase within polyurethane foam. Energy Fuels
2009, 23:5725-5730.
39. Epton R, Hobson ME, Marr G: Synthesis and properties of
expanded poly(acryloyl morpholine)/carbonic anhydrase
conjugates with catalytic activity in aqueousorganic media.
Polymer 1977, 18:1203-1207.
40. Billsten P, Freskgard PO, Carlsson U, Jonsson BH, Elwing H:
Adsorption to silica nanoparticles of human carbonic
anhydrase II and truncated forms induce a molten-globule-like
structure. FEBS Lett 1997, 402:67-72.
41. Yadav R, Satyanarayanan T, Kotwal S, Rayalu S: Enhanced
carbonation reaction using chitosan-based carbonic
anhydrase nanoparticles. Curr Sci 2011, 100:520-524.
www.sciencedirect.com
42. Gitlin I, Gudiksen K, Whitesides G: Peracetylated bovine
 carbonic anhydrase (BCA-Ac18) is kinetically more stable than
native BCA to sodium dodecyl sulfate. J Phys Chem B 2006,
110:2372-2377.
Report on chemical modification of carbonic anhydrase to enhance its
kinetic stability.
43. Ramachandran PA, Chaudhari RV: Three Phase Catalytic Reactors.
New York: Gordon and Breach Science Publishers; 1993.
44. Derks PWJ, Kleingeld T, Aken Cv, Hogendoorn JA, Versteeg GF:
Kinetics of absorption of carbon dioxide in aqueous
piperazine solutions. Chem Eng Sci 2006, 61:6837-6854.
45. Fradette S, Gingras J, Voyer N, Carley J, Kelly GR, Ceperkovic O:
Process for CO2 capture using micro-particles comprising
biocatalysts. US Patent WO11014956; 2011.
46. Trachtenberg MC, Bao L, Smith DA, Dumortier R: Low energy,
low cost, efficient CO2 capture. 8th International Conference in
Green House Gas Control Technologies. Trondheim, Norway:
International Energy Agency; 2006.
47. Trachtenberg MC: Novel enzyme compositions for
removing carbon dioxide from a mixed gas. US Patent
US20080003662; 2008.
48. Zhang YT, Zhang L, Chen HL, Zhang HM: Selective separation of
low concentration CO2 using hydrogel immobilized CA
enzyme based hollow fiber membrane reactors. Chem Eng Sci
2010, 65:3199-3207.
49. Lee S-W, Park S-B, Jeong S-K, Lim K-S, Lee S-H,
Trachtenberg MC: On carbon dioxide storage based on
biomineralization strategies. Micron 2010, 41:273-282.
50. Swanson E, Patel T, Banta S, Brady P, Davis K, Park A-HA:
Chemical and biological catalytic enhancement of weathering
of silicate minerals. NETL/DOE 2010 CO2 Capture Technology
Meeting. Pittsburgh, PA: NETL; 2010.
Current Opinion in Biotechnology 2011, 22:818823