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org/journal/ascecg Research Article

Carbonic Anhydrase Immobilized on Textile Structured Packing

Using Chitosan Entrapment for CO2 Capture
Jialong Shen, Yue Yuan, and Sonja Salmon*
Cite This: https://doi.org/10.1021/acssuschemeng.2c02545 Read Online

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ABSTRACT: Innovative carbon dioxide (CO2) capture ap-

proaches are urgently needed to lower and reverse CO2 emissions
that lead to climate change. Here, we report the design, fabrication
and testing of high efficiency biocatalytic textile-based gas−liquid
contactors made using versatile, sustainable, and readily available
polymers, cellulose, and chitosan, together with an immobilized
carbonic anhydrase (CA) enzyme to accelerate CO2 absorption
into benign, low-energy, aqueous potassium carbonate (K2CO3)-
based solvents. This novel structured packing is able to withstand
the CO2 scrubbing environment, will be simple to scale up, and
will be useful as a “drop-in” for conventional chemical absorption
systems as well as offer new possibilities for direct air capture.
Immobilizing CA in a thin coating on textile packing surfaces
minimizes the enzyme requirement, retains enzyme in the absorber for high catalytic benefit and longevity with repeated use, and
allows downstream process flexibility by preventing CA from traveling to other unit operations, for example, high temperature
desorption where enzyme could become inactivated. CA immobilization on cotton fiber textile packing materials by entrapment with
chitosan exhibited an activity recovery of at least 49% and activity retentions of higher than 68% after 10 repeated wash and retest
cycles over 5 days and up to 41% after a 31 day incubation in 10 wt % K2CO3 at 40 °C. The lightweight biocatalytic textile packing
modules are sturdy and easily handled with no sharp edges or dusting issues as can accompany conventional metal packing- or
particulate-immobilized enzymes. In laboratory-scale countercurrent CO2 absorption tests at 4 L per minute total gas flow rates, CA-
immobilized textile packings delivered average CO2 absorption efficiencies of 52.3% and 81.7% for single and double-stacked
packings, respectively, versus 26.6% and 46.4% for single and double-stacked no-enzyme control textile packings, and versus 3.6% for
conventional glass Raschig rings filled to the equivalent single-stacked packing height. Textile packings exhibited excellent solvent
distribution throughout the packing even at low liquid flow rates, maintaining uniform gas contact with the wetted solid contacting
surfaces across a range of different liquid flow rates, leading to robust CO2 capture efficiency. Biocatalytic textile packing retained
66% of the initial CO2 capture performance after five cycles of washing, drying, ambient storage, and retesting over a period of 66
days. In a separate test with freshly made packing, 76.5% performance retention was observed after a continuous 120 h recirculation
longevity test.
KEYWORDS: Immobilized carbonic anhydrase, Biocatalytic textiles, Enzyme, Structured packing, Chemical absorption, CO2 capture

■ INTRODUCTION
Anthropogenic carbon dioxide (CO2) is the major contributor
combustion power plant flue gasis chemical absorption,3
where monoethanolamine (MEA) is the most commonly used
to the greenhouse effect and climate change. Nearly 70% of it benchmark solvent.4 Despite MEA’s high capture efficiency
is emitted from the generation of electricity, heating, and and fast absorption kinetics, a steep energy penalty for
transportation.1 For reliability and avoiding expensive replace- regeneration accounting for up to 60% of the total operating
ment costs in transitioning into a net-zero emission energy cost5 makes it less than desirable. Numerous studies have
system, some long-lived capital assets such as existing CO2 sought alternative solvents with lower regeneration energy, for
emitting coal-, natural gas-, or biomass-fired power plants need
to be retrofitted with carbon capture and sequestration for Received: April 28, 2022
continued service before other nonemitting power generation Revised: May 18, 2022
technologies catch up with the ever increasing energy
consumption needs.2
Currently, the most mature technology to capture CO2 at
atmospheric pressurethe condition relevant for most

© XXXX American Chemical Society https://doi.org/10.1021/acssuschemeng.2c02545

A ACS Sustainable Chem. Eng. XXXX, XXX, XXX−XXX
ACS Sustainable Chemistry & Engineering
example, methyldiethanolamine (MDEA) and potassium
carbonate, which in turn come with their own challenge of
having slower absorption kinetics.6 Carbonic anhydrase (CA),
a rate-enhancing biocatalyst with low environmental impact,
has attracted much attention in the development of low energy
CO2 capture technologies.7,8 Adding CA into low regeneration
energy solvents enhances the CO2 absorption rate and holds
the promise of a reduced capital cost enabled by smaller
equipment size and a reduced operation cost from the solvent
regeneration.9−11 However, frequent enzyme replenishment
could be required due to thermal denaturation of the
enzyme12,13 when passing through the high temperature
desorber. Alternatively, immobilizing and confining CA
enzymes in the lower temperature absorber, where CA
contributes significant reaction rate enhancement, would
minimize thermal deactivation, would improve longevity, and
could reduce cost. Extensive literature is available on
immobilizing CA on various physical supports with varying
degrees of success. These efforts were largely summarized in a
number of recent review papers.14−18 However, essential
design and demonstration of the processes that would allow for
a simple drop-in application of biocatalysts in the existing
chemical absorption system, such as that designed for the MEA
process, are rare in the literature. In one notable study,
Reardon et al. (Akermin Inc.)19 used a sol−gel process to
encapsulate CA in an organosilica20 matrix that was coated on
commercial stainless-steel structured packings. A field test with
these packings exhibited a 6- to 7-fold adsorption rate
enhancement for a carbonate-based solvent at 40 °C with an
average CO2 capture efficiency of 80% on coal flue gas.
Preliminary techno-economic analysis (TEA) indicated a 6.5%
reduction in incremental cost of electricity (ICOE) relative to
the reference case of 30% MEA. Additionally, considering
improved interaction at the gas−liquid interface, prediction
was made for up to 30.9% reduction in ICOE when CA is
immobilized in buoyant mobile silica-based microparticles
instead of being fixed on stationary structured packings. The
concept of mobile CA-immobilized microparticles21 was later
demonstrated in a small demo-scale unit where a 6-fold
enhancement in CO2 absorption versus 30% MDEA alone was
achieved, and a simple “add-on” biocatalyst recycling
mechanism based on the buoyancy of the microparticles in
the solvent was proposed.22 Nevertheless, challenges still exist
in maximizing the gas−liquid−biocatalyst contacting area,
minimizing mass transfer barriers, and reducing the cost, all of
which must be overcome to advance the performance of
immobilized CA for CO2 capture.
We herein report the design, fabrication, and testing of a
novel biocatalytic gas−liquid contactor that meets the
following critical criteria: (1) Packing material selection aligns
with the sustainability profile of enzymes and is expected to
withstand the CO2 scrubbing environment. (2) Packing raw
material sources and fabrication costs are anticipated to be low,
and the design allows for simple scale-up and drop-in
application in existing chemical absorption systems. (3)
Materials provide the necessary functionality and abundance
of surface areas to allow for subsequent immobilization of
enzymes and enhancing liquid transport on and inside the
packing to maximize the gas−liquid contact area. (4) CA-
immobilized packing enhances CO2 absorption, reducing the
amount of CA needed in the system and extends CA
performance longevity by protecting it from exposure to
potential high temperatures in the desorption process.
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Naturally derived polysaccharides, for example, cellulose and
chitosan, are attractive support materials for enzyme
immobilization23 owing to their natural abundance, biodegrad-
ability, and availability of reactive sites for functionaliza-
tion.24−27 Recently, we reported a robust biocatalytic textile
yarn28 flow-through reactor that is capable of decomposing at
least a double amount of peroxide with a 20-fold reduction in
reaction zone volume compared to a typical stirred tank
reactor. The structural function of the textile yarn not only
provides ease of fabrication and handling but also serves as a
conduit for controlled liquid flow within the yarns. Encouraged
by this result, we adapted this enzyme entrapment matrix
system to immobilization of CA on textile-based packings.
Such packings could be fabricated at industrial-scale leveraging
existing textile processing machinery to produce a multitude of
biocatalytically functional fibrous materials from one-dimen-
sional fibers and yarns to two-dimentional fabrics, and all the
way to three-dimensional packing structures. Compared to
many other potential fabrication components, cotton and
chitosan are readily available and have good tolerance to
alkaline conditions.29,30 In summary, the enzyme entrapment
system selected for this study meets all requirements stated in
the criteria above, and this report demonstrates the excellent
CO2 capture efficiency enhancement and performance
longevity achieved by the novel packing design and enzyme
immobilization protocols of the biocatalytic textile packings.
■ EXPERIMENTAL SECTION
Materials. Chitosan (ChitoClear 44020−fg95LV; degree of
deacetylation = 95%; viscosity of 21 cP at 1% chitosan concentration)
was purchased from Primex EHF, Iceland. Cheesecloth 90 grade
fabric (100% cotton) was purchased from Testfabrics, Inc. (West
Pittston, NJ). The 50/50 polyester/cotton latch hook canvas (5
mesh; center-to-center distance per opening ∼5.2 mm; yarn thickness
∼1.2 mm; opening size ∼4 mm; IG Design Group Americas, Inc.,
Atlanta, GA) was purchased from a local crafts store. Raschig rings
(CG-1283-01, borosilicate glass, 8 mm × 8 mm) were purchased from
Chemglass, Inc. (Vineland, NJ). Acetic acid (Glacial, Certified ACS,
Fisher Chemical), hydrochloric acid solution (1N certified, Fisher
Chemical), 4-nitrophenol (99.0+%, TCI America), 4-nitrophenyl
acetate (Alfa Aesar, 98+%, Thermo Scientific), ethanol (Absolute, 200
Proof, molecular biology grade, Fisher BioReagents), potassium
carbonate (anhydrous, granular powder/certified ACS, Fisher
Chemical), potassium bicarbonate (cryst./certified ACS, Fisher
Chemical), and glutaraldehyde (50% aq. soln., Alfa Aesar) were
purchased from Fisher Scientific, USA. Trizma base (primary standard
and buffer, ≥99.9% by titration, crystalline), N-methyldiethanolamine
(≥99%, Sigma-Aldrich), and phosphate-buffered saline tablets (0.01
M phosphate buffer, 0.0027 M potassium chloride and 0.137 M
sodium chloride, pH 7.4, at 25 °C) were purchased from Millipore-
Sigma, USA. Carbonic anhydrase (experimental thermostable micro-
bial CA, concentrated liquid solution with esterase activity of 18.8 U/
mL measured according to the method described herein) was
obtained from Novozymes A/S, (Bagsvaerd, Denmark) and is referred
to as NZCA in our discussion. All chemicals were used as received
without further purification.
Instrumentation. For Fourier-transform infrared spectroscopy
(FTIR), a Nicolet Nexus 470 spectrometer (ThermoFisher Scientific,
USA) was equipped with a Nicolet OMNI germanium crystal
attenuated total reflection (ATR) sampling head. All specimens were
air-dried and stored at laboratory conditions before measurement. A
total of 64 scans were collected for each sample spectrum with a
resolution of 4 cm−1, and backgrounds were collected before the first
measurement and once every 30 min thereafter. For scanning electron
microscopy (SEM), an Hitachi TM 4000 desktop SEM unit operated
in backscattered electrons mode, secondary electrons mode, or a mix
of the two and at an accelerating voltage of 10 kV was used to observe
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the surface morphology of the fibrous materials coated with a gold/
palladium sputter coating. Water contact angle (WCA) measurement,
conducted with an FDS OCA 15 Pro Video-based optical contact
angle measuring instrument (DataPhysics Instruments USA Corp.),
was used to evaluate the wettability of the immobilized enzyme
biocatalytic textiles, no-enzyme controls, and model thin films cast on
glass slides. A UV−vis spectrophotometer (TECAN Spark Microplate
Reader, TECAN, USA) was used to measure the absorbance of
colored products generated during assays for calculating enzyme
activities. A dry shaker bath (Thermoscientific MaxQ 2000) equipped
with a J-KEM 3300 temperature controller was used to carry out
solvent and heat stress tests of the biocatalytic textiles.
Preparation of Coating Solution. Chitosan powder was first
dissolved in 5 v/v% acetic acid in a deionized (DI) water solution at a
concentration of 5 w/v%, and the dissolved solution (pH ∼ 2) was
poured into a casting plate for air-drying over a two-day period. After
the solvent evaporated, a protonated chitosan film was obtained and
was redissolved immediately (excess air drying renders the film harder
to redissolve) in DI water at a concentration of 1 w/v%. The chitosan
solution thus prepared (mild pH of ∼5) was used to coat no-enzyme
textile controls. For enzyme immobilization, NZCA liquid was slowly
added into the pH 5 chitosan solution at varying concentrations with
continuous stirring. Ratios of 1:0.05−1:2 chitosan:NZCA (g:mL) in
the solution were explored in this study.
Coating Hydrophilic Textile Support Materials. Hydrophilic
textile support materials were coated using the solutions described
above by either a dip-coating method or a solution padding process
(Supporting Information Figure SI-1). Dip-coating was achieved by
immersing and completely wetting the selected textile materials in a
solution bath with the help of mild mechanical agitation and the
inherent hydrophilicity of the textile fibers. Excess solution was then
squeezed out manually or using a mechanical press (pad mangle) to
the desired percent wet pickup. In the solution padding process, the
selected textile materials were wetted and squeezed simultaneously
between a pair of rollers pushed tightly against each other forming a
solution reservoir for wetting and squeezing out excess solution as the
textile materials exit the padder. The percent wet pickup was
controlled through adjustment of the roller pressure. A typical drying
process for the wet-coated textile materials involved air-drying at
room temperature on a drying rack for 2 days.
CA Esterase Activity Assay. Adaptation and modification of CA
assays to enable analytical comparison between dissolved and
immobilized CA and to evaluate biocatalyst robustness for material
optimization and rapid screening purposes was necessary. Two
different assays are commonly used for measuring dissolved CA
activity: one based on fast CO2 hydration and the other on slow ester
hydrolysis. Because many CA enzyme variants exhibit “diffusion
limited” reaction kinetics,9 meaning that the main catalytic reaction of
CO2 hydration itself is so fast that the experimental rate-limiting step
becomes the mixing efficiency, we anticipated that the mixing
efficiency for homogeneous systems of dissolved enzyme and
substrate would be faster than for heterogeneous systems of solid
immobilized enzyme and dissolved substrate. In heterogeneous
systems, parameters such as enzyme localization and exposure of
enzyme active sites to dissolved substrates can impact the measured
apparent enzyme activity. Therefore, the conventional Wilbur−
Anderson (W-A) type assay,31 which measures fast CO2 hydration
using dissolved CO2 as the substrate, was found to be unsuitable for
measuring the activity of immobilized CAs (exceptions include CAs
immobilized on particles that can be dispersed as a suspension, which
behave like dissolved CAs). The NZCA used in this study is capable
of hydrolyzing p-nitrophenylacetate (pNPAc), making its activity
detectable by the slower ester hydrolysis reaction. Hence, the pNPAc
esterase activity assay was selected to measure the apparent enzyme
activity of CA after immobilization, enabling the detection of enzyme
activity that is otherwise inaccessible to the fast assay due to diffusion
limits.
The adaptation needed for measuring solid samples essentially
involved modifying the assay to use 24-well plates, where the well size
is sufficiently large to accommodate a piece of biocatalytic textile
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sample. Depending on their dimensions, textile samples could either
be coiled at the well perimeter or cut into a doughnut shape with an
outside diameter of 5/8 in. and an inner diameter of 5/32 in. for the
signal light to pass through (Supporting Information Figure SI-2a).
Four replicates of each sample were placed in one column of the 24-
well plate. The pNPAc substrate was first dissolved in ethanol to
prepare a 100 mM stock solution. Then, immediately before starting
each set of measurements, the stock solution was diluted to a final
concentration of 8 mM in deionized water. A Tris buffer (950 μL of
25 mM, pH 7.2) and 50 μL of diluted pNPAc substrate were added to
each well containing solid textile samples (with or without
immobilized CA). For dissolved CA activity, the enzyme sample
was first diluted in 25 mM Tris buffer (pH 7.2); then, 950 μL of the
dilution was added to each empty well along with 50 μL of diluted
pNPAc substrate. After brief gentle manual mixing, the 24-well plate
was inserted into a TECAN Spark microplate reader and incubated
for 5 min at 25 °C before beginning absorbance measurements at 405
nm, once every 30 s for 30−60 min. Active CA catalyzes the
hydrolysis of pNPAc into p-nitrophenol (pNP), which is yellow
colored and has a maximum absorbance peak at 405 nm.
Development of a more intense yellow color during the assay
indicates higher CA enzyme activity (Supporting Information Figure
SI-2b). When the O.D. values (at 405 nm) are plotted against time in
minutes, the slope of the curve is the O.D. change per minute
(Supporting Information Figure SI-3). A standard curve relating the
O.D. value to known amounts of pNP standard prepared in the same
buffer was established (Supporting Information Figure SI-4). Using
the slope of the pNP standard curve, the pNP release rate with a unit
of nmol/min is obtained. For the contribution made by the enzyme,
the rate for the Tris buffer (or corresponding no-enzyme textile
control) is subtracted from the rate of the sample. One unit of CA
esterase activity is defined as the amount of enzyme that catalyzes the
release of 1 μmol of pNP per minute from the substrate at 25 °C (U =
μmol/min) (Supporting Information SI−C for details).
Assay-Scale Longevity Test. Biocatalytic textiles samples were
tested repeatedly using the CA esterase activity assay described above.
Between subsequent measurements, the assay solution from the
previous run was replaced with two changes of fresh buffer solution
before resuming the next measurement. The activity of each sample,
normalized against the corresponding initial activity, was expressed as
percent activity retention and plotted as a function of assay sequence
number. A total of 10−11 cycles were repeated over 5 days for each
assay plate. In addition, the samples with a chitosan:NZCA (g:mL)
ratio of 1:0.8 were continued with heat and solvent stress testing in 30
wt % MDEA. Briefly, four doughnut-shaped replicates of the same
sample were grouped and immersed into 5 mL of aqueous 30 wt %
MDEA solution (pH 10.4) in a 20 mL glass vial and placed in the dry
shaker bath, set at an orbital shaking rate of 100 rpm. Temperatures
were increased in a stepwise manner, each maintained for a 3 day
period. Then, samples were separated from the solvent and rinsed
thoroughly on a Buchner funnel with water and buffer at the end of
each incubation period before being assayed for their esterase
activities. After each assay run, samples were rinsed thoroughly with
the buffer and water and wicked dry by Kimwipe paper before being
reimmersed in 5 mL 30 wt % MDEA. Additionally, a set of samples
with a chitosan:NZCA (g:mL) ratio of 1:1 was made and tested in a
similar manner as the MDEA solvent stress test but with 10 wt %
K2CO3 (pH ∼ 10.5) and at a constant temperature of 40 °C for a
period of 31 days.
Fabrication of Textile Structured Packing. Textile packings
can be fabricated using either the coated materials prepared using the
method described in the previous section or using the uncoated raw
materials and then coating the preformed packings in their final forms.
Assembling three-dimensional packing modules with pristine cotton
cheesecloth before subjecting each completed module to dip-coating
simplifies material handling at the lab scale. After exploring several
different designs, a “jelly roll”-like spiral design with an outer diameter
of 6 cm and a nominal height of 22.5 cm was selected for these
evaluations based on its superior preliminary CO2 capture efficiency
compared to other designs tested (Supporting Information Figure SI-
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ACS Sustainable Chemistry & Engineering
5). Packing modules were made using rigid low-water-absorbing latch
hook canvas that serves as structural reinforcement and spacer
material and using flexible absorbent cheesecloth that acts as the
primary matrix for solution uptake and enzyme entrapment. The
mesh construction throughout the packing module, even at the top
and bottom edges which were denser due to the spacers, allowed
sufficient gaps and holes for gas to pass through. At the low gas flow
rates used in these studies, column flooding did not occur. A
cheesecloth “cone” at the bottom of the packing aided in directing
liquid flow to exit the bottom center of the spiral and forced gas to
pass through several layers of cheesecloth before entering the spiral
packing. The completed assembly rested firmly against the lower
packing support lip of the glass absorber column, ensuring that gas
would pass upward through the packing (Supporting Information
Figure SI-6).
Dip-Coating Preformed Textile Packings. Coating of the
preformed textile packings was performed in a 1 L graduated cylinder
that permits complete immersion of the packing in the solution
(Supporting Information Figure SI-7). Typically, the packings were
dipped and drained repeatedly three times over a total of 15 min of
immersion time to allow for complete wetting and coating of all
available surfaces. Two replicates were dip-coated with chitosan
without enzymes (no-enzyme control), and another two were dip-
coated with a chitosan solution containing NZCA loading of 1:1
(g:mL, chitosan:NZCA solution) (enzyme packing). To examine the
effects of NZCA loading and liquid-to-gas (L/G) ratio on the packing
CO2 capture efficiency, one additional packing was made for each
additional chitosan:NZCA ratio. The wet-coated textile packings were
hung and air-dried at room temperature for a period of 2 days. Cross-
linking was performed on one of the packing preparations (1:2 ratio)
to counteract premature enzyme leaching that could lead to lower
performance during continuous scrubber operation. Briefly, the
freshly coated and dried packing was placed in a 1 L graduated
cylinder along with 1 L of PBS buffer (pH 7.4) containing 0.2 v/v%
glutaraldehyde and stirred magnetically for 3 h. The cross-linked
packing was rinsed with copious DI water, soaked in 1 L Tris buffer
(25 mM, pH 7.4) overnight to cap reactive free aldehyde groups, and
then rinsed under tap water to remove excess Tris buffer before air
drying.
Laboratory Gas Scrubber Setup and Operation. The
laboratory gas scrubber was operated in single-pass flow-through
absorption mode, meaning that lean fresh solvent was delivered to the
top of the column and flowed downward through the packing
installed in the column where it came into countercurrent contact
with a prehumidified defined gas mixture that entered at the bottom
of the column and flowed upward through the packing (Supporting
Information Figure SI-8). The volume percent composition of the gas
mixture delivered to the bottom of the column was controlled by
setting the flow rate of two mass flow controllers, one for CO2 and
one for N2, that were located upstream of a gas mixing chamber. The
premixed gas then passed through a controlled temperature gas
humidifier before entering the absorber column. The system was
operated at near ambient temperature (20−23 °C). The absorber was
fitted with one or two 6 cm inner diameter and 30 cm long glass
columns, depending on the experiment (Supporting Information
Figure SI-6). After exiting the top of the column, the gas stream was
analyzed by a CO2 gas analyzer equipped with an active sample pump
that drew a portion of the wet exit gas through a gas drying column
before entering the gas analyzer IR detector. The remaining portion of
the wet gas stream was vented into the chemical fume hood duct. All
packings were presoaked in the scrubbing solvent for 10 min before
being installed in the absorber column to improve reproducibility and
minimize the possibility of uneven wetting during the experimental
run.
CO2 Capture Efficiencies of Textile Packings. Nominal 10 wt
% K2CO3 solvent (K2CO3/KHCO3 weight ratio of 85/15, pH 10.5)
was used as a model CO2 scrubbing solvent and was delivered at 120
mL/min for the scrubber test with a total gas flow rate of 4 L/min
(0.4 L/min CO2 and 3.6 L/min N2). Two pairs of packings were
tested in the following order: (1) each of the two replicate no-enzyme
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controls, one after the other, to gauge reproducibility of fabrication,
(2) stacking two control packings, one on top of the other, to
demonstrate the stackability and continuity of gas−liquid contact,
both physically and in terms of the resulting enhancement, (3) and
(4) repeat the same sequence for the immobilized enzyme packing
replicates as those described in (1) and (2) for the controls, and (5)
Raschig ring random packings filled in the glass column up to the
same packing height, as a reference for comparison. Because Raschig
rings cannot support themselves like the textile packings do, a 2 mm
square mesh stainless steel wire screen was used at the bottom of the
column to support the rings. In a separate experiment using the same
conditions, uncoated textile packing was tested with NZCA dissolved
in the scrubbing solvent at concentrations of 0.37 and 1.375 mL/L as
positive controls.
In some published studies, CO2 capture efficiency (or percent of
CO2 removal) has been calculated according to eq 1, based on the
CO2 concentrations of the inlet and exit gases19
CO2in − CO2out
× 100%
CO2in (1 − CO2out ) (1)
where CO2in is the CO2 concentration at inlet, and CO2out is the CO2
concentration at outlet. In other reports, eq 1 is simplified32 as
CO2in − CO2out
× 100%
CO2in (2)
Equation 2 eliminates the additional term accounting for the
volume of CO2 that has been captured, which results in a more
conservative CO2 capture efficiency with up to 3% underestimation.
This is within the experimental error of the current work, which uses a
maximum measured starting CO2 percent concentration of ∼11.1%.
Therefore, eq 2 was used to calculate the more conservative values of
CO2 percent presented in this study (Supporting Information Figure
SI-9.). Because CO2 percent at the inlet of our lab-scale scrubber does
not change over time, as it may in real flue gas, only one CO2 analyzer
was required at the exit, and the inlet concentration was taken to be
the stabilized CO2 concentration measured (also at exit) before
turning on the scrubbing liquid flow. To evaluate the effect of the L/G
ratio, liquid flow rates of 120, 72, 24, and 13 mL/min were used,
corresponding to L/G ratios of 30, 18, 6, and 3.3 mL/L, respectively.
The longevity of the biocatalytic packing was evaluated by retesting
the CO2 capture efficiency after each test−wash−dry−storage cycle
spanning over a period of 66 days. Dry storage of packing modules
between tests was at room temperature. Additional longevity testing
was carried out for a freshly made replicate enzyme-immobilized
packing in a continuous 120 h solvent recirculation experiment where
room temperature 10 wt % K2CO3 flowed through the packing for the
entire duration of the experiment. The CO2/N2 gas mixture described
above was delivered to the absorber column periodically to obtain
CO2 capture efficiency measurements at different time intervals.
During these measurements, solvent recirculation was stopped, and
fresh lean solvent was passed through the absorber.
■ RESULTS AND DISCUSSION
Surface Chemistry, Morphology, and Wettability.
Cotton cheesecloth grade 90, a fabric with a convenient
balance of yarn density for structural stability and interyarn
porosity for allowing gas and liquid flow, was selected as model
textile fabric for testing various coating methods and
conditions. First, tests were conducted to confirm the
successful entrapment of enzymes inside the coating layer on
the surface of the physical support and to observe
morphological or wettability changes resulting from the
coating process. Although only contributing a small fraction
of the weight of the physical support material, the presence of
enzyme on the biocatalytic textiles was confirmed spectro-
scopically by comparing the differences in peak intensities of
characteristic functional groups in FTIR spectra. Overall, all
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Figure 1. FTIR spectra of chitosan-coated no-enzyme control, chitosan:NZCA 1:1 coated, chitosan:NZCA 1:2 coated, and neat cheesecloth 90.
spectra reflect and resemble the underlying physical support
cellulose material, which makes up a substantial mass fraction
of the biocatalytic textiles. All absorbance spectra were
normalized against each spectrum’s maximum absorbance
value around 1058 cm−1, which represents the C−O−C
vibration in the backbone ring structure.33 By doing so, the
changes in the intensities of the peaks among different samples
could be compared. In particular, peaks near 1650 cm−1 were
assigned to strong CO stretching (amide I) in the protein
amide groups.34 The spectra in the vicinity are expanded in the
inset of Figure 1. As expected, the two enzyme-immobilized
samples exhibited higher IR absorption intensities near 1650
cm−1. The small peak in the same region for neat cheesecloth
or chitosan-coated cheesecloth can be attributed to the H−O−
H bending of absorbed water.33,35 Peaks near 1540 cm−1 are
commonly referred to as the amide II band, which is
attributable to the combination of C−N stretching and N−
H bending. Samples with entrapped enzyme proteins had
much higher peak intensities in this region, as expected, while
chitosan coating itself also contributed to the peak intensity, as
evidenced by the comparison between neat cheesecloth and
chitosan-coated cheesecloth. Another region, centered around
3300 cm−1 representing O−H (or N−H from chitosan or
enzyme protein) stretching, exhibited notable differences
among samples but in a nearly reversed order to that for the
1650 cm−1 region. The number of O−H bonds in the chemical
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structure of cellulose should be proportional to the number of
repeating units or pyranose rings. The difference in the peak
intensity is due in part to the frequency (or wavenumber)
dependence of the penetration length of the IR light in the
ATR technique, where at a larger wavenumber the penetration
length is much shorter and therefore only able to interact with
the outermost layers (larger proportion of chitosan and
enzyme) of the biocatalytic textiles, in comparison to that at
around 1058 cm−1 whose peak intensity was determined by
interactions deeper into bulk of the materials, making this a
suitable reference for normalization. Additionally, our prior
study found that the moisture content of pristine cotton yarn
(7.3%) decreased significantly after being coated with chitosan
(1.29%−1.34%), while remaining unaltered (7.1%−7.5%) after
physical enzyme adsorption without chitosan.28 In view of this
prior observation, the reduction in the vibrational peak
intensities near 3300 cm−1 may also be a manifestation of
the reduced amount of water absorbed on cheesecloth after
treatment with chitosan and entrapped enzymes. Further
discussion of the hydrophobic behavior of chitosan coating is
included below and in a supplemental section on water contact
angle (Supporting Information SI-H).
The structural parameters and morphologies of the cheese-
cloth after being coated with chitosan with or without NZCA
were characterized using SEM. The cheesecloth fabric has a
loose plain weave fabric construction with an average square
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Figure 2. SEM images of (a) and (b) dip-coated 1% chitosan on cheesecloth 90 air-dried and (c) and (d) dip-coated 1% chitosan with enzyme
loading of Chitosan:NZCA 1:1 on cheesecloth 90 air-dried.

opening size of 433 ± 54 μm. The average diameter of the Table 1. Fabrication Parameters of Biocatalytic Textiles and
cotton yarns was 220 ± 53 μm, and individual cotton fibers Their Resultant Activity Recovery
making up the cotton yarn have an average width of 15 ± 4
Chitosan Wet Activity
μm. As shown in Figure 2(a) and (b), the air-dried chitosan- concentration pickup recovery
coated no-enzyme control showed smooth fiber surfaces, as do Method (%) Chitosan:NZCA (%) (%)
the enzyme-entrapped samples shown in Figure 2(c) and (d). Dip-coating 1 1:0.05 402.3 49.2
There were no chitosan or NZCA aggregates observed Dip-coating 1 1:0.1 437.3 71.7
between the interstitial spaces of the fabric opening or in Dip-coating 1 1:0.2 431.6 71.6
between the cotton fibers within the yarn, indicating that the Dip-coating 1 1:0.4 382.0 57.4
thin coating was on the single fiber level. The excellent coating Dip-coating 1 1:0.8 375.8 75.6
quality of chitosan on cellulose is attributable to electrostatic Padding 1 1:1 137.3 62.1
attraction between the positively charged chitosan at mild Padding 1 1:1 176.4 50.5
acidic conditions and the naturally anionic cellulose as well as Padding 1 1:1 150.0 61.5
specific polymer−polymer interactions arising from the
similarity in the chemical structures of the two polysacchar- longevity of the biocatalytic textiles. The presence of the thin
ides.36 In an order-of-magnitude estimation, dip-coated chitosan coating was also detectable by instantaneous water
chitosan would generate a thin coating with a thickness on contact angle (WCA) measurements. The as-received cotton
the order of 44 nm, while the padded sample would yield a cheesecloth 90 absorbed water droplets instantaneously (WCA
coating thickness of around 17 nm. Values used in this = 0°), while the chitosan coated samples, with or without
estimation are cotton specific surface area37 of 0.8 m2/g, entrapped NZCA, had instant (t < 3 s) water contact angles in
chitosan film density38 of 1.13 g/cm3, and wet pickups of the hydrophobic range of 126°−134° (Supporting Information
approximately 400% and 150% for dip-coating and padding, Figure SI-10). All samples wetted out fully over time. Since
respectively (Table 1). Since carbonic anhydrases have WCA is extremely sensitive to surface chemistry and
diameters on the order of 5 nm,39 the thin 44 and 17 nm roughness, which, as observed here, caused transient hydro-
coatings should minimize mass transfer barriers for efficient phobic effects, model thin, flat films were cast directly on clean
catalytic function while being sufficiently thick to fully entrap glass slides to observe the impact of the different chitosan
enzymes in the chitosan matrix in a way that could extend formulations. The more protonated film made from chitosan
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acetic acid solution (pH ∼ 2) had the lowest WCA of 62°, and
the film made from the less protonated DI water dilution (pH
∼ 5) had the highest WCA of 99°. Adding NZCA to the pH 5
solution resulted in a film with an intermediate WCA of 74°,
indicating that a portion of enzymes entrapped in the film
could be partially exposed to the solid liquid interface. Partially
exposed enzymes should be beneficial for obtaining a higher
CO2 capture efficiency by reducing mass transfer barriers
imposed by the chitosan matrix, although too much surface
exposure could also lead to leaching.
Immobilization Quality and Reusability. A lab-scale
dip-coating method was used to test the enzyme entrapment
capability of chitosan on cheesecloth. Here, 1 w/v% mild pH
chitosan solutions (pH ∼ 5, prepared by redissolving
protonated chitosan film in DI water) with chitosan-to-
NZCA ratios ranging from 1:0.05 to 1:0.8 were employed in
this experiment. Fabrication parameters and their resultant
activity recoveries are listed in Table 1. Owing to the
hydrophilic nature of cotton, the wet pickup of the fabric Figure 3. Activity retention of dip-coated biocatalytic textiles after
during the dip-coating process was quite high at about 400% of repeated buffer washing and testing.
the weight of the fabric. After 2 days of air drying on a rack,
fabric samples were cut into doughnut shapes to fit the 24-well Table 1, padded entrapment prototypes achieved 51%−62%
assay plate used for esterase activity assay. Activity recovery, activity compared to an equal amount of dissolved NZCA.
which is the percentage of the activity of the immobilized After 10 cycles of repeated buffer washing and testing, these
enzyme compared against the starting activity of the same padded entrapment samples retained 71%−77% of their
amount of enzyme in its dissolved form, was used to evaluate original activity over 5 days, meaning that padding catalytic
the quality of the immobilization process. Activity recovery chitosan coating on cellulosic fabrics can be an efficient
after immobilization varied from 49% to up to 76% across the approach in manufacturing the CA-immobilized textiles
entire NZCA concentration range explored. The variability in (Figure 4).
activity recovery across all dip-coated samples is likely a result
of the manual lab-scale fabrication method. This activity
recovery range compares favorably with other CA immobiliza-
tion studies, including 5%−31% when immobilized on a
hydrophilic−superhydrophobic “Janus” membrane,40 56.3%
when encapsulated in an alginate hydrogel bead,41 20%−55%
when immobilized on PVDF composite hollow fiber
membranes,42 32% when conjugated with liposome,43 and
75% when immobilized on a mesoporous cruciate flower-like
metal organic framework.44 In the current study, increasing the
NZCA loading does not sacrifice the outstanding activity
recovery afforded by the chitosan matrix. Even at a 1:0.8
chitosan to NZCA solution ratio, the maximum loading
capability of chitosan was not reached as indicated by the
absence of a decreasing trend of activity recovery with
increasing enzyme loading. Variable enzyme loading coupled
with sufficiently high activity recovery provides vast flexibility
in tailoring biocatalytic textile formulation and fabrication to
Figure 4. Activity retention of padded biocatalytic textiles after
meet up-scaling requirements. As shown in Figure 3, all
repeated buffer washing and testing.
samples regardless of their loading amounts demonstrated
good reusability, with activity retention varying between 68%
and 78% at the end of 11 sequential repeated washes in pH 7.2 Heat and Solvent Stress Tests of Immobilized NZCAs.
buffer and tests over 5 days. Assay-scale simulations of practical conditions encountered in
One method that could be relevant for industrial-scale the absorber were made by incubating samples in 10 wt %
fabrication of enzyme-immobilized textiles involves the use of K2CO3 (pH 10.5) at a constant temperature of 40 °C and with
textile padding equipment. This method can enhance the constant shaking. As shown in Figure 5, enzyme activities
efficiency of raw material utilization during material dropped significantly during the first 3−4 days of incubation
production. Because a NZCA loading ratio of 1:0.8 (g:mL, followed by a gradual loss of activity over time. The
chitosan:NZCA solution) did not reach its maximum loading comparison between curves from testing separate samples
capacity, the loading was increased to 1:1 (g:mL, chito- each day and testing the same samples over and over after
san:NZCA solution) in the fabrication of padded enzyme- repeated incubate−wash−test cycles emphasizes the deterio-
entrapped textile prototypes. By varying the roller pressure, rating effect of additional wash and handling. Each point on
different wet pickup values were obtained that directly the black curve represents independently incubated samples
correlated with the amount of NZCA loading. As listed in with only one wash and filtering before activity testing. The
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Figure 5. Heat and solvent stress test of dip-coated sample
(chitosan:NZCA ratio of 1:1) in 10 wt % K2CO3 at 40 °C with
100 rpm orbital shaking.
points on the red curve represent the activities of single
samples being repeatedly incubated, washed, and filtered for an
incremental number of times. After 31 days of incubation in
the 10 wt % K2CO3 solvent at 40 °C with 100 rpm orbital
shaking, the black curve shows a 41.5% activity retention. In
contrast, the red curve only shows 6.0% of the original activity
remaining at the end of 31 days incubation, indicating the
activity loss during the repeated washing and filtering steps.
These two curves can be viewed as the upper and lower
boundaries between which the actual activity retention of the
packing should reside. In actual continuous scrubber
application, the enzyme activity retention would be more
closely represented by the black curve, as the trickling effect of
the solvent is relatively mild compared to the repeated
vigorous tap water wash and dry cycles (red curve). A similar
heat and solvent tolerance test was carried out with an
alternative solvent, 30 wt % MDEA, except that the incubation
temperature was increased stepwise. As shown in Figure 6, the
immobilized NZCAs were compatible with 30 wt % MDEA at
Figure 6. Heat and solvent stress test of dip-coated sample
(chitosan:NZCA ratio of 1:0.8) in 30 wt % MDEA with incremental
temperature increase and 100 rpm orbital shaking.
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room temperature. This is consistent with Leimbrink et al.’s
finding21 that CA immobilized in organosilica microparticles
showed no loss of activity over a total of 16 weeks of
immersion in 30 wt % MDEA at 20 °C. As temperature and
accumulated time immersed in the solvent increased, the
measured activities decreased. The 75% activity retention after
a continuous 3 days at room temperature (RT) and an
additional 3 days at 40 °C immersed in 30 wt % MDEA (pH
10.4) demonstrate a useful longevity level for absorber packing
applications, which are typically maintained at around 40 °C.13
For comparison, Shao et al.45 recently reported 30%−60%
activity retention when carbonic anhydrase was immobilized in
zeolitic imidazolate framework particles and incubated in 1 M
MDEA for 9 days at 40 °C, with the conclusion that
entrapping enzyme made it more tolerant to solvent, and
Zhang et al.46 reported that CA immobilized on a similar
zeolitic framework material increased the enzyme activity by
1.5 times compared to free CA enzyme and retained ∼75%
activity after 20 days incubation in 1 M MDEA at 40 °C,
whereas free CA enzyme only retained 54% activity at those
conditions. Considering that our tests were conducted in 30 wt
% MDEA (∼2.5 M), versus the published tests in 1 M MDEA,
NZCA immobilized on textiles has comparable activity
retention to other reported materials. For potential application
of these types of packings in the desorber, system robustness
would need to be improved using further developed
immobilization strategies and potentially more thermo-tolerant
CA enzymes. Textiles as immobilization supports are
promising in these applications because they can retain their
mechanical properties during extended exposure to CO2
scrubbing solvents. For example, reference cotton fabric
samples that were incubated in 30 wt % MDEA or 23 wt %
K2CO3 (solubility limit) solvents for 78 days at room
temperature (∼20 °C) retained their full tensile strength
relative to soaking in water (Supporting Information SI−I and
Figure SI-11).
CO2 Absorption Tests in Laboratory Gas Scrubber. To
maximize gas−liquid contact surfaces, avoid column flooding,
and direct liquid flow uniformly through the packing volume, a
spiral textile-based packing design was made by integrating
continuous spiral-shaped contacting surfaces within the rolled-
up walls of vertical contacting surfaces. Two replicates of
preformed packings were dip-coated with chitosan without
enzymes (no-enzyme control), and another two were dip-
coated with a chitosan solution containing NZCA loading of
1:1 (g:mL chitosan:NZCA solution) (enzyme packing). The
variabilities in CO2 absorption results caused by hand
fabrication of replicate packings were small, and thus, an
averaged curve was plotted for each packing preparation. As
shown in Figure 7, glass Raschig ring packing only provided
minimal CO2 absorption capacity compared to textile packings
with or without enzyme. Specifically, standard Raschig rings
filled in the column to a 22.5 cm height only sustained a 3.6%
CO2 absorption from the total CO2 amount going through the
column, while no-enzyme control textile packing and enzyme-
immobilized textile packing delivered average absorption
efficiencies of 26.6% and 52.3%, respectively. When two
packings were stacked together, effectively increasing gas
molecule residence time, the two no-enzyme controls reached
a 46.4% capture efficiency, while the two enzyme packings
achieved a higher capture efficiency of 81.7%. This is close to
the 84.5% delivered by an uncoated textile packing assisted by
a dose of dissolved NZCA (0.37 mL/L) that was
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Figure 7. CO2 capture efficiency of textile packings in a laboratory CO2 gas scrubber.
approximately equivalent, over the time period of the test, to
the amount of enzyme as was immobilized on each enzyme
packing. Notably, the initial increase in CO2 capture efficiency
versus time for the dissolved enzyme had a delayed response,
on par with the no-enzyme control, compared to the
immobilized enzyme packing. This is because enzymes
dissolved in the solvent are only effective in accelerating the
CO2 absorption when they are located at the gas−liquid
interfaces. Only after dissolved enzymes have thoroughly
wetted the textile structured packing were they sufficiently
distributed at the gas−liquid−solid contacting surfaces to
achieve a high level of CO2 capture efficiency enhancement. In
comparison, the immobilized enzymes acted immediately
because they were prepositioned on fiber surfaces at the
gas−liquid interface, leading to faster CO2 absorption
response. The advantages of using immobilized enzymes for
a recirculating absorption−desorption system are apparent
when compared to the scenario where dissolved enzymes
would be exposed to the desorber temperature (>100 °C) and
lose activity, requiring continuous replenishment. In order to
keep the same level of CO2 capture in the dissolved enzyme
system, more enzymes are needed as the experiment run time
increases. Thus, the net enzyme savings increases with
increasing run time and increasing longevity of immobilized
enzymes. Nevertheless, even at the short run time of 12.5 min
(equivalent point for the enzyme amount used), the average
CO2 capture efficiency for a single enzyme-immobilized
packing module already reached 63% of the CO2 capture
efficiency obtained by an equivalent amount of dissolved
enzymes. An even higher CO2 absorption efficiency of 94.5%
was achieved (result not plotted in the figure) by a higher dose
of dissolved NZCA (1.375 mL/L) flowing through an
uncoated textile packing. This better performance of the
dissolved enzyme originates from its mobility toward liquid gas
interfaces where the absorption reaction takes place,
significantly reducing the diffusion limitation of CO2 molecules
traveling to the active sites of the CA. The soluble enzyme
reference values demonstrate that with high enough enzyme
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dosing and an optimized enzyme distribution inside the
packing through structural design (including fine structure and
high gas−liquid surface area creation), it will be possible to
further improve CO2 absorption performance of enzyme-
immobilized packing.
Effects of Enzyme Loading on CO2 Capture Efficiency.
Considering esterase assay test results, the continued increase
of p-NP release rate with increasing enzyme loading indicated
the absence of a plateau up to a chitosan:NZCA ratio of 1:0.8,
which constituted the basis for choosing a 1:1 ratio for the
initial benchmarking tests. However, the esterase assay uses a
different and irrelevant (in the context of CO2 capture)
substrate (an ester as opposed to CO2) as well as operates at
markedly different (longer) time scale compared to the CO2
hydration reaction. Therefore, while the esterase assay is able
to reveal the amount of active enzyme present on the textile
physical support, this result is not directly translatable to the
activity of CO2 hydration reaction in the gas scrubber because
the long reaction time obscures potentially rate limiting mass
transfer barriers of the immobilization matrix. Hence,
fabricating and testing enzyme-immobilized textile packings
with different enzyme loadings in the laboratory gas scrubber is
necessary. As shown in Figure 8, the increase of NZCA loading
from chitosan:NZCA 1:0.25 to 1:0.5 resulted in a significant
enhancement in the CO2 capture efficiency, while the increase
from 1:0.5 to 1:2 yielded lesser improvement. The fact that
increasing the amount of enzyme present in the bulk of the
chitosan matrix from 1:0.5 to 1:2 does not significantly
improve the CO2 capture efficiency suggests that immobilized
enzyme on or near the surface of the chitosan matrix on the
fibers plays a dominating role in accelerating CO2 absorption
into the solvent in a realistic gas scrubber system.
Effect of Solvent and Gas Flow Rates on CO2 Capture
Efficiency. In addition to solvent type, solvent concentration,
and CO2 concentration, CO2 capture efficiencies of the
packings also depend on both the solvent and gas flow rates.
To characterize solvent and gas flow rates, a liquid-to-gas or “L
over G” (L/G) ratio is a commonly used variable in the
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Figure 8. Effect of enzyme loading on the CO2 capture efficiency of
the biocatalytic textile packings.
discussion of CO2 capture efficiency. In this experiment, the
solvent flow rates were varied from 120 to 13 mL/min at a
constant total gas flow rate of 4 L/min, which resulted in L/G
ranging from 30 to 3.3 mL/L (Figure 9). Irrespective of the
Figure 9. Effect of L/G on the CO2 capture efficiency of biocatalytic
textile packings.
enzyme loading, decreasing the L/G ratio from 30 to 6 mL/L
resulted in a relatively gradual decline in the CO2 capture
efficiency, while a dramatic drop was observed going from 6 to
3.3 mL/L, at which point the limited amount of solvent
flowing through the packing was overwhelmed (saturated). In
other words, the textile packings were able to operate at a low
L/G of ∼6 mL/L without a drastic decrease in the capture
efficiency. The exact L/G number where the precipitous
performance drop occurs will depend on operational
parameters such as solvent type and concentration, column
diameter and height, CO2 concentration of the feed gas stream,
and other variables. Nevertheless, the result presented here
demonstrates that the textile packing is capable of distributing
solvent efficiently throughout the packing, even at very low
liquid flow rates, and maintains uniform gas contact with the
wetted solid contacting surfaces across a range of different
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liquid flow rates, leading to robust CO2 capture efficiency.
Provided that the CO2 loading capacity of the solvent is not
exceeded, operating the CO2 absorber at a low L/G can be
desirable for minimizing the amount of solvent that needs to
be heated during the CO2 stripping process, thereby saving
energy. Importantly, no column flooding and no wall effects
(no liquid running along the inside surface of the column)
were observed at any of the test conditions, meaning that the
packing allowed excellent liquid and gas transport through the
column.
A comparison of the textile packings with different amounts
of entrapped NZCA confirmed that conclusions drawn from
results obtained at the regular 120 mL/min solvent flow rate
also held true at lower flow rates. Essentially, increasing
enzyme loading beyond a 1:0.5 (chitosan:NZCA) ratio only
had a modest benefit in terms of increasing the CO2 capture
efficiency. Therefore, the chitosan to NZCA ratio can be
optimized for performance and minimized to reduce material
consumption. It is also evident in Figure 9 that the textile
packing with entrapped NZCA loading of chitosan:NZCA 1:2
exhibited a larger relative decrease in CO2 capture efficiency as
the experiment proceeded from higher to lower flow rates.
Potentially, enzyme loading in this preparation exceeded
chitosan’s entrapping capability, resulting in enzyme on or
near the surface being not bound as securely and being washed
away in the flowing solvent by leaching. A postentrapment
chemical cross-linking treatment was employed with this
coating recipe to explore the effect of cross-linking on the CO2
capture efficiency of the textile packing. CO2 capture efficiency
for cross-linked and uncross-linked packings were almost
identical at an L/G of 30 mL/L, which was tested first. As
testing continued to lower L/G ratios, cross-linked packing
performed better, which may be explained by enzyme leaching
from the uncross-linked packing as the testing proceeded. This
successful utilization of a cross-linking agent to minimize
enzyme leaching provides a path for future work to extend the
longevity of textile packings.
Reusability and Longevity of Enzyme-Immobilized
Textile Structured Packing. As emphasized earlier, the
material savings brought about by enzyme immobilization
depends on its reusability and longevity. After the first scrubber
test, NZCA-immobilized textile packings were rinsed in cold,
low-hardness tap water to remove solvent, allowed to air-dry,
and stored open to air at ambient lab conditions. After 24 days
of storage, all of the textile packings were retested a second
time. The CO2 capture efficiencies of the enzyme-immobilized
textile packings dropped slightly for both of the replicates
tested individually (from 50.5% to 48.6% and from 56.0% to
45.5%) and for two of them stacked together (from 81.7% to
73.0%). These results indicate that a small portion of the
enzyme activity was lost during the use, rinsing, and storage
steps. However, as shown in Figure 10which shows the CO2
capture efficiency changes of one of the two enzyme-
immobilized textile packings and no-enzyme control packings
over five cycles of washing, drying, and retesting intermittently
over a period of 66 daysthe reused packing remained highly
active in accelerating CO2 absorption into the scrubbing
solvent. The CO 2 capture efficiency of the enzyme-
immobilized packing dropped from 50.5% in its first run to
33.3% in its fifth run (retention of 66% performance). Notably,
the no-enzyme textile packing (control) yielded very consistent
capture efficiency of 23%−24% using the same 10 wt % K2CO3
solvent in the first, second, and last scrubber tests. Thus,
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Figure 10. CO2 capture efficiency of biocatalytic textile packing and
no-enzyme control after repeated washing, drying, and retesting over a
period of 66 days. Runs #3 and #4 used different solvent
concentrations than the regular 10 wt % K2CO3.
differences observed in tests bracketed by the two, namely,
third and fourth using 20 and 5 wt % K2CO3, respectively, can
be attributed to differences in solvent alone. Increasing the
solvent concentration to 20 wt % reduced the capture
efficiency of the uncatalyzed absorptions as well as the
catalyzed absorptions, as evidenced by the precipitous drop
in performance. This is because the higher viscosity of the
concentrated solvent changed liquid flow behavior and/or
increased liquid film thickness, which led to reduction in gas−
liquid-enzyme interfaces and decreased the overall absorption
performance. However, reducing the concentration of K2CO3
from 10 to 5 wt % did not affect the CO2 capture efficiency of
the uncatalyzed absorption process, whereas the catalyzed
absorption was negatively impacted (comparing runs #4 and
#5). An explanation for this is as follows: because of the higher
capture efficiency resulting from the performance of the
enzyme, the 5 wt % K2CO3 solvent may have exceeded its CO2
loading capacity and therefore showed a lower capture
efficiency compared to the more concentrated 10 wt %
K2CO3. Some level of enzyme leaching between the sequential
trials may have also been a factor.
In addition to the batchwise test−wash−dry cycles, a
separate replicate of the packing was made and installed in
the scrubber for a 120 h continuous recirculation and retesting
experiment. In this new experiment, room temperature solvent
flowed through the packing for the entire duration of the
experiment, and the CO2 capture efficiency was measured at
different time intervals. As shown in Figure 11, the enzyme-
immobilized packing exhibited a significant drop in CO2
capture efficiency during the first 8 h of continuous solvent
flow, whereas no meaningful change in the CO2 capture
performance was observed during the subsequent 100 and
more hours. The ending CO2 capture efficiency at 120 h was
39.1%, constituting 76.8% retention of the initial efficiency of
50.9%. The continuous run was then stopped and the packing
washed with tap water and air-dried. This enzyme entrapped
packing was tested a second time 21 days later, and the capture
efficiency dropped to 33.0%. This behavior is consistent with
the assay-scale longevity test result discussed previously in that
burst leaching of enzyme occurred in both cases at the early
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Figure 11. Continuous 120 h scrubber recirculation longevity test
with 10 wt % K2CO3 solvent at room temperature.
stages of the tests and that additional washing and handling
caused further decrease in performance. These results provide
a benchmark for improving the performance. While the effects
on enzyme longevity of other gas components that could be
present in industrial flue gas streams (e.g., SOx, NOx, N2O, O2,
CH4) were not evaluated in this study, according to the
literature, CA-based capture systems could tolerate the
presence of gas impurities that may remain after conventional
upstream pollution controls.9
■
CONCLUSIONS
We designed and fabricated a novel biocatalytic textile-based
gas−liquid contactor structured packing using sustainable,
readily available cellulosic and chitosan materials that are able
to withstand the CO2 scrubbing environment, will be simple to
scale up, and could be used as a “drop-in” for current
commercial-scale chemical absorption systems.
The successful entrapment of enzyme on the surface of the
physical support, confirmed by FTIR and SEM observations,
indicated that chitosan coats individual cotton fibers as a very
thin layer, leaving the individual fiber shapes intact and well
separated to expose the coated surfaces. An order-of-
magnitude estimation revealed that the dip-coated chitosan
would generate a thin coating with a thickness on the order of
44 nm, while the padded sample would yield a coating
thickness of 17 nm, both of which are thin enough to avoid
prohibitive mass transfer barriers while also sufficiently thick to
be able to securely entrap enzyme. The chitosan-coated
samples have instant water contact angles in the hydrophobic
range of 126°−134° but are all wettable over time. Model thin
films cast directly on clean glass slides showed that the more
protonated film made from chitosan acetic acid solution had
the lowest WCA of 62°, and the redissolved-recast film using
DI water (higher polymer solution pH and hence less
protonation on the chitosan polymer) had the highest WCA
of 99°. Adding entrapped NZCA slightly reduced the WCA of
the thin film to 74°, indicating that a portion of the enzyme
could be partially embedded with hydrophilic exteriors
exposed.
Activity recoveries from 49% to 76% and 51% to 62% were
achieved by dip-coated and padded samples, respectively. All
samples regardless of their loading amounts demonstrated
good reusability, with activity retention of 68% to 78% and 71
to 77% for dip-coated and padded samples, respectively, after
10−11 cycles over 5 days. Heat and solvent stress tests
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revealed a 75% activity retention after being immersed in 30 wt
% MDEA for 3 days at room temperature (RT) and an
additional 3 days at 40 °C, demonstrating a good longevity at
absorber relevant conditions. A 31 day heat and solvent stress
test in 10 wt % K2CO3 at 40 °C revealed activity retentions of
6.0% and 41.5% for samples with and without repeated
additional washing and filtering, respectively.
In laboratory CO2 gas scrubber tests, no-enzyme control
textile packings and enzyme-immobilized textile packings
delivered average CO2 absorption efficiencies of 26.6% and
52.3%, respectively, a significant improvement over the 3.6%
obtained using glass Raschig ring random packing filling the
same volume. The stackability of textile packings was
demonstrated as the two no-enzyme controls reached a
46.4% CO2 capture efficiency, while the two enzyme packings
achieved a higher capture efficiency of 81.7%. The high capture
efficiency of the novel biocatalytic textile structured packing
along with the stackability create the potential for using a
shorter absorption column to achieve a desired level of CO2
capture, which would help reduce overall CO2 capture capital
costs. Increasing NZCA loading from chitosan:NZCA 1:0.25
to 1:0.5 resulted in a significant enhancement in CO2 capture
efficiency, while an increase from 1:0.5 to 1:2 yielded only
minimal improvement. This implies that immobilized enzyme
on or near the surface of the chitosan matrix on the fibers plays
a dominating role in accelerating CO2 absorption into the
solvent in a realistic gas scrubber system. The textile packings
were able to operate at a low L/G of ∼6 mL/L without a
drastic decrease in the capture efficiency. It was demonstrated
that the textile packing is capable of distributing solvent
efficiently throughout the packing even at low liquid flow rates,
maintaining uniform gas contact with the wetted solid
contacting surfaces across a range of different liquid flow
rates, leading to robust CO2 capture efficiency. Operating the
CO2 absorber at a low L/G can be desirable for minimizing the
amount of solvent that needs to be heated during the CO2
stripping process, thereby saving operational cost. The CO2
capture efficiency of the enzyme-immobilized packing retained
66% of its initial performance after five cycles of washing,
drying, and retesting over a period of 66 days. A continuous
120 h recirculation longevity test revealed that leaching of
immobilized enzyme from the packing occurred as a burst
during the first 8 h of continuous operation, and thereafter, the
packing retained a stable CO2 capture efficiency that was
76.8% of the initial capture efficiency by the end of the test.
The successful utilization of a cross-linking agent in minimizing
enzyme leaching provides a route for future work to extend the
longevity of textile packings.
The findings herein demonstrate that immobilizing CA on
novel textile-based structural packing provides enhanced CO2
absorption, reduces the needed amount of CA in the system,
and extends the longevity of CA performance by protecting it
from stresses that could be encountered outside the absorber
environment. On the basis of the unique properties of the
biocatalytic textile packing presented here, we anticipate a wide
applicability of the biocatalytic textile CO2 capture system in
emerging and growing carbon capture and sequestration
applications, such as postcombustion capture, natural gas and
biogas upgrading, CO2 removal from industrial process gases,
CO2 capture from bioenergy power plants, or CO2 capture
from air, i.e., direct air capture. In the meantime, scale-up of
biocatalytic textile packings is in progress for bench-scale
testing which will be published in our subsequent studies.
L https://doi.org/10.1021/acssuschemeng.2c02545
■
pubs.acs.org/journal/ascecg Research Article
ASSOCIATED CONTENT
* Supporting Information
sı
The Supporting Information is available free of charge at
https://pubs.acs.org/doi/10.1021/acssuschemeng.2c02545.
Solution padding process, CA esterase activity assay
method, calculation of CA esterase activity values,
justification of the selected formula for CO2 capture
efficiency, illustration for fabrication of textile structured
packing, schematic of laboratory gas scrubber setup and
operation, illustration of enzyme immobilization process,
discussion of water contact angle results, and tensile
strength of reference cotton fabric (PDF)
■ AUTHOR INFORMATION
Corresponding Author
Sonja Salmon − Department of Textile Engineering, Chemistry
and Science, Wilson College of Textiles, North Carolina State
University, Raleigh, North Carolina 27695-8301, United
States; orcid.org/0000-0003-2477-9023;
Email: sisalmon@ncsu.edu
Authors
Jialong Shen − Department of Textile Engineering, Chemistry
and Science, Wilson College of Textiles, North Carolina State
University, Raleigh, North Carolina 27695-8301, United
States; orcid.org/0000-0002-8692-4663
Yue Yuan − Department of Textile Engineering, Chemistry and
Science, Wilson College of Textiles, North Carolina State
University, Raleigh, North Carolina 27695-8301, United
States
Complete contact information is available at:
https://pubs.acs.org/10.1021/acssuschemeng.2c02545
Author Contributions
The manuscript was written through contributions of all
authors. All authors have given approval to the final version of
the manuscript.
Notes
The authors declare no competing financial interest.
■
ACKNOWLEDGMENTS
This work was made possible by funding from North Carolina
State University (NCSU) and from the Alliance for Sustainable
Energy, LLC, Managing and Operating Contractor for the
National Renewable Energy Laboratory (NREL) for the U.S.
Department of Energy through the BETO project WBS
5.1.3.103 “Novel Cell-free Enzymatic Systems for CO2
Capture”, a collaboration between NREL, NCSU, and the
University of Kentucky’s Center for Applied Energy Research
(UK-CAER), utilizing enzymes provided by Novozymes. The
authors would like to thank Avery Padula for conducting
tensile tests, Judy Elson for taking SEM images, and Birgit
Andersen for her assistance with measuring water contact
angles.
■
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