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Patent US20040259231 - Enzyme facilitated solubilization of carbon dioxide from emission streams in ... - Google PatentsucheSuche Bilder Maps Play YouTube News Gmail Drive Mehr »AnmeldenPatentsucheThis invention pertains to a novel biotechnological process of solubilization and concentration of CO2 from emission exhausts or streams that could be coupled for further biochemical/chemical conversion. The biotechnological process occurs in novel reactors/devices employing immobilized biocatalysts...http://www.google.de/patents/US20040259231?utm_source=gb-gplus-sharePatent US20040259231 - Enzyme facilitated solubilization of carbon dioxide from emission streams in novel attachable reactors/devices Erweiterte PatentsucheTry the new Google Patents, with machine-classified Google Scholar results, and Japanese and South Korean patents. VeröffentlichungsnummerUS20040259231 A1PublikationstypAnmeldung AnmeldenummerUS 10/464,789 Veröffentlichungsdatum23. Dez. 2004Eingetragen18. Juni 2003 Prioritätsdatum18. Juni 2003Auch veröffentlicht unterUS20050214936 Veröffentlichungsnummer10464789, 464789, US 2004/0259231 A1, US 2004/259231 A1, US 20040259231 A1, US 20040259231A1, US 2004259231 A1, US 2004259231A1, US-A1-20040259231, US-A1-2004259231, US2004/0259231A1, US2004/259231A1, US20040259231 A1, US20040259231A1, US2004259231 A1, US2004259231A1 ErfinderSanjoy BhattacharyaUrsprünglich BevollmächtigterBhattacharya Sanjoy K.Zitat exportierenBiBTeX, EndNote, RefMan Referenziert von (66), Klassifizierungen (7) Externe Links: USPTO, USPTO-Zuordnung, EspacenetEnzyme facilitated solubilization of carbon dioxide from emission streams in novel attachable reactors/devices
US 20040259231 A1 Zusammenfassung
This invention pertains to a novel biotechnological process of solubilization and concentration of CO2 from emission exhausts or streams that could be coupled for further biochemical/chemical conversion. The biotechnological process occurs in novel reactors/devices employing immobilized biocatalysts enabling concentration and solubilization of emitted CO2 by allowing catalytic contacting with water spray. These novel reactors or devices could be coupled to other reactors/devices resulting in further biochemical/chemical conversion of the concentrated carbon dioxide. Bilder(16) Ansprüche(2)
DETAILED DESCRIPTION OF THE INVENTION [0018] This invention pertains to a biotechnological process or method whereby the carbon dioxide present in the emission stream (free of soot) could be contacted with water in the presence of immobilized carbonic anhydrase resulting in catalytic solubilization of carbon dioxide in water. The enzyme, carbonic anhydrase is immobilized on glass, polystyrene or silica coated steel matrix using DCC or carboxyl coupling described elsewhere (Bhattacharya, et. al., 2003). The contacting process of gas with water also results in the concentration of CO2 from emission stream in the aqueous phase. The process operation and measurement methods are described in further detail below after a brief physical description of the reactor(s). Description of the Reactor(s) [0019] The biotechnological process described above occurs in a novel immobilized carbonic anhydrase (CA) reactor that has been designed and is also an integral part of this invention. This reactor(s) has the highly porous immobilized CA within its core and allows flow of emission gases and water in the form of spray. The reactor parts described in this section pertain to FIGS. 1 and 2. The gas in the reactor enters through a tube connected directly to the emission stream (part 1 in FIGS. 1 and 2). [Not shown here, the highly porous filter offering negligible resistance that holds macroscopic soot and countercurrent water flow across the connector tube bringing the emission gas to the reactor, the treatments needed prior to actual emission stream entry to the reactor cores. The prior treatment renders emission gas free of soot and brings the temperature between 60-80° C. suitable for operation of this biotechnological process, and not being claimed as part of the invention]. The top of the reactor has a lid (part 2), connected with water entry port (part 3) and the bottom of this top portion has a porous lid that allows water spray (part 4). The novel trickling spray reactor has a solid body (part 5), which houses the central immobilized matrix shell (part 7). The shell is encased in a wire mesh (part 6) and sits on a perforated metal plated coated with glass (part 9). The pores in the metal plate (part 9) are 2-5 mm in diameter sits on a strand (part 10) and does not offer mass transfer or flow resistance to aqueous solution/suspension that flows through it. The reactor has one entry port (part 1) and one exit port (part 8) for the flow of emission gas/stream. The emission entry port is either vertical entering from the top or from the horizontal side (FIG. 1, 2). The reactor also has water inlet (part 3), spray mechanism (part 4) and water/solution outlet (part 11). The bottom of the reactor (part 12) usually collects the aqueous flow and through a single tubing exit (part 11). This solution exit (part 11) could easily be connected with a coupled immobilized Rubisco reactor. The dimension of the cylindrical central part of the reactor is 50 cm×30 cm (diameter×length). The diameter of the gas inflow and outflow tube is 10 cm. However, these dimensions can vary according to the emission stream and other parameters. The 5 cm from the top of this cylindrical central reactor houses water for spray. The water inlet (part 3) and solution outlet (part 11) has a diameter of 2 cm. The spray is governed by lid having pores of diameter 0.5 mm (part 4). The wire mesh encasing (part 6) for immobilized enzyme is made up of steel material having pores with diameter of 5-8 cm. The steel is coated with glass to withstand corrosion. [0020] Reactor Operation and Stability of the Immobilized Biocatalyst. [0021] The reactor described above houses the immobilized enzyme core. The carbonic anhydrase from thermophilic Methanobacterium thermoautotrophicum was cloned in pET19b vector using standard molecular biology protocols as described elsewhere (Smith and Ferry, 1999) was used in the reactor core. Some experiments were also performed using previously reported cloned human carbonic anhydrase IV in pET11d (Waheed et. al., 1997). The enzymes were immobilized on glass, polystyrene or silica coated steel matrix of different average mesh size using methods as reported earlier (Bhattacharya et. al., 2003). The novelty of this biotechnological process lies is using the immobilized enzyme in porous matrix and using water spray instead of solution phase enzyme so that mass transfer resistance to the emission gas is negligible. A thin film of water around the enzyme in the immobilized microenvironment keeps the enzyme hydrated and active for a long time and the buffering of the enzyme apparently is not necessary for a long period. A flush with buffer every third day of continuous operation greatly enhances the shelf-life of the immobilized enzyme. The reactor design, which is the other novel part of this invention, has three basic designs. The reactors in all three designs provide ability to control two different flows, flow of emission gas and that of water spray, with respect to flow of gases it is either horizontal inflow and horizontal outflow or vertical inflow and horizontal outflow (or vice versa). With respect to water spray it was either vertical or horizontal. Therefore basic design of the reactor were reduced to three different types (a) with horizontal inflow and outflow of gas and vertical water spray, (b) vertical inflow, horizontal outflow of gas (or vice versa) and vertical water spray and (c) vertical inflow, horizontal outflow of gas (or vice versa) and horizontal water spray (FIG. 1 & 2 A, B, C). The designs that employed vertical inflow of gas, allowed the inflow only from the top but never from the bottom. This is due to stability of matrix in presence of vertical inflow from the bottom and also the bottom gas inflow would lead to water spray going to the emission stream at least in some design settings. This process and reactor(s) allowing the catalytic contacting of carbon dioxide with water would enable concentration and solubilization and feeding the solubilized CO2 into coupled fixation bioreactors (Bhattacharya, 2001) and is expected to serve as a great utility. While the prior art exists on enzyme immobilization but there is absolutely no description of contacting carbon dioxide (or emission gas) with water in presence of porous immobilized carbonic anhydrase or anything similar as described in this biotechnological process in printed literature or electronic resources makes this a novel utility. In all these studies simulated stack emission was used generated using a mixture of gases and carbon dioxide derived from dry ice. However, we envisage, based on the operation studies that the device/reactors will work with different emissions including stack emissions. The method using in construction of the device or in measurements are described in the experimental protocol section. The reactor operation optimization studies with respect to different parameters are described below. [0022] Effect of emission flow rates and CO2 content in the emission gas on CO2 reduction. The simulated emission stream where CO2 percent in the stream was manipulated using gas from dry ice with varying flow rates (having carbon dioxide accounting for about 33-40 percent of the stream) was subjected to treatment using an enzymatic core having an average enzyme load of 1.5 mg/ml. The water flow rate was held constant at 2.5 ml/min mean matrix pore size was 1 μm. As shown in FIG. 3, the reduction in CO2 initially increased reaching a plateau between 5-7 L/min and the decreases progressively. At each point the CO2 in the stream without any treatment (without attachment of the reactor core) was treated as 100 percent, based on which a decrease in CO2 was calculated. The reduction in CO2 was also measured using an artificially enriched stream of CO2. At a flow of 4.5 L/min with immobilized enzyme load of 1.5 mg/ml there was a progressive increase in the reduction of CO2 in the emission stream, which reached a plateau when the carbon dioxide concentration in the emission stream reached around 70 percent (FIG. 3). [0023] Effect of spray area versus immobilized core volume on CO2 reduction. The area of spray with respect to core immobilized CA volume affected percent CO2 reduction, when this biotechnological process was used. In order to understand the effect of spray area to the volume of immobilized enzyme core, the diameter of the core was varied while keeping the volume constant (100 ml). The resultant L/D ratio was calculated and percent CO2 reduced was determined, where L refers to length and D refers to diameter of the core (FIG. 1). As shown in FIG. 4 the L/D ratio had an effect on CO2 reduction the either extreme of L/D ratio led to a decrease in reduction. The higher length reduced the mass transfer where as the lower length led to decrease solubilization and rapid escape of carbon dioxide from the immobilized CA core. The intermediate L/D ratio was optimal for proper mass transfer to the active site of CA and hold up of the gas within the immobilized core. [0024] Effect of flow rate of water (spray) on CO2 reduction. The rate of water flow due to the spray also affected the catalytic solubilization of CO2. Fast flow of water enabled a constant hydration and availed sufficient water near the active site for catalytic conversion. Flow rate of water was varied from 1 ml/min to 12.5 ml/min. The increase in water flow rate showed an initial increase in the rate of CO2 reduction and reached a plateau around 8 ml/min (FIG. 5). The availability of water around the immobilized CA affected the CO2 reduction, which is manifested by increase in reduction with increased flow rate. However, after the flow rate passes limiting rate any further increase in water does not allow further availability of reacting aqueous phase near the active site of enzyme thereby the rate remains unaffected. [0025] Effect of enzyme load on CO2 reduction. Immobilized enzyme load had a profound effect on reduction of carbon dioxide. The enzyme load was varied from 0.25 to 10 mg/ml. There was a progressive increase in CO2 reduction up to 5 mg/ml of enzyme load and beyond this there was a decrease in the CO2 reduction from the emission stream. The decrease is perhaps due to denaturation of enzyme as well as mass transfer limitation in the enzyme microenvironment with high protein load (FIG. 6). [0026] Effect of Immobilized matrix pore size on CO2 reduction. The matrix pore size influences CO2 reduction. The average matrix pore size, varied between 0.5 to 5 μm, was determined by mercury intrusion porosimetry utilizing an Aminco-Winslow Porosimeter (Messing, 1970; Messing, 1974) described in experimental protocols. The increase in pore size increases the reduction but beyond a definite size (2 μm) further increase in pore size actually reduces the CO2 reduction (FIG. 7). The increase in CO2 reduction with increased pore size is due to increase mass transfer of CO2 near the active site of immobilized carbonic anhydrase. The observed decrease in CO2 reduction with large pore size is perhaps due to escape of carbon dioxide from reaching to actual active site of the enzyme immobilized in such matrix. Also the availability of water and diffused carbon dioxide at the same rate in the large pore size matrix may affect the rate of CO2 reduction. [0027] The attachment of the reactor module in the emission stream and pressure drop across the stream. The attachment of the reactor is expected to bring a change in the pressure of outlet (after the reactor) and inlet (before the reactor) within the gas emission. In order to test this, the emission gas pressure before entry to the reactor and at the exit port of the reactor was determined with respect to thickness of reactor core and with varying matix pores using HD8804 K pressure and temperature kit equipped with appropriate pressure probes and also using Testo 525 instrument (Hotek Technologies, Tacoma Wash.). The reactor inlet stream without any reactor connection maintained at a pressure of about 104 Pa. However, we have also used a very high-pressure simulated system for these investigation (data not shown), where we have observed insignificant pressure changes due to attachment of reactors. Using reactor cores of varying diameter (100 to 1000 cm; FIG. 8) as well as matrix pores of 0.5 to 5 μm pressure was measured in the reactor inlet and outlet (FIG. 9). The maximum pressure drop was only 17 percent for more than for an immobilized reactor core with diameter of 1000 cm. The pressure drop in the outlet or back-pressure (that is, pressure increase in the inlet) in the inlet was less than 11 percent till 500 cm core diameter. A commensurate but insignificant increase in inlet pressure (back pressure) was also observed when immobilized reactor core was added (FIG. 8). Using a reactor vessel without an immobilized core water flow alone did not show a significant effect on inlet or outlet pressures (data not shown). The matrix pore size also had an effect on pressure. However the pressure drop with 0.5 μm matrix pore was only about 10.5 percent than without any reactor core control (FIG. 9). The average matrix pore size of 2 μm offered only 5 percent decrease in pressure in the outlet. Decrease in pore size led to increased drop in pressure in the outlet and increased pressure in the inlet. However, the pressure drop in the outlet was less than 11 percent with moderate pore size (FIG. 9). [0028] The efficiency of the single versus multiple reactors for CO2 reduction. The multiple reactors (FIG. 10A) with incremental volume (FIG. 10B) added up to a reactor (FIG. 10A) with equal combined volume (Figure B) were better in reducing the CO2 from the emission stream than a single reactor with equal combined volume. Using four reactors of 250 ml and a single reactor of 1000 ml it has been found that the multiple reactors provided better extraction/reduction of CO2 (FIGS. 10A & B). Using this enzymatic reactors it was found that CO2 could be extracted from emission stream much in the same fashion that solvent extraction is done for organics. Thus using multiple reactors, reduction of carbon dioxide roughly obeys the equation: Amr =A(KV 1 /KV 1 +V 2)n [0029] K: distribution coefficient for carbon dioxide; K=Cgas/Csoution [0030] Amr: the amount of CO2 left in the emission stream after n reactors [0031] A: the amount of CO2 in the stream without any reactor [0032] V1: the volume of emission gas used [0033] V2: the volume of water used for solvation of CO2 in each reactor [0034] Experimental Procedures: [0035] Carbonic anhydrase. The carbonic anhydrase from thermophilic Methanobacterium thermoautotrophicum was cloned in pET19b vector using standard molecular biology protocols as described elsewhere (Smith and Ferry, 1999). The cloned enzyme was expressed in E. coli BL21DE3 plysS transformed with a plasmid vector (pET19b) carrying the DNA sequence and purified using Ni-NTA resin column and was used in the reactor core after immobilization. Recombinant human CA isoform IV which was also used in identical studies was purified using E. coli BL21DE3 plysS transformed with a plasmid vector (pET 11d) carrying the DNA sequence of human CA IV, kindly provided by Dr. William Sly as research gift. The enzyme was expressed and purified following published protocols (Waheed et. al., 1997). The bovine and human erythrocyte carbonic anhydrase were procured from Sigma Chemical Co., St. Louis, Mo. [0036] Assay of Carbonic anhydrase. Carbonic anhydrase was activity was assayed using an electrometric method (Wilbur and Anderson, 1948). A 50 μl protein solution was diluted to 4 ml of pre-chilled 50 mM HEPES (N-2-hydroxethylpiperazine-N′-ethanesulfonic acid) buffer, pH 8.0. For assay at different pH, 50 mM HEPES was used above pH 7.0 and 50 mM MES (2N-morpholinoethanesulfonic acid) below pH 7.0 were used. The mixture was stirred and maintained on ice for several minutes. The assay was initiated by the addition of 10 ml of ice-cold, CO2-saturated water into the reaction vessel. The change in pH from 8.0 to 7.0 at 25° C. was monitored using a bench top pH meter and semi-micro combination electrode and the signal was directed to a chart recorder. CA activity is expressed in Wilbur-Anderson (WA) units per mg of protein and was calculated using the formula [(t0/t−1)×10]/mg protein, where t0 and t represent the time required for the pH to change from 8.0 to 7.0 in a buffer control and CA sample respectively. A micromethod was also used to determine CA activity for some selected samples (Maren, 1960) to determine whether the activity measured with electrometric method have good correlation. [0037] Immobilization. The carbonic anhydrase was immobilized using different coupling methods on steel matrix coated with glass, polystyrene or silica (Bhattacharya et. al. 2003). [0038] Preparation of the Silanized Carrier. The iron fillings from a lathe machine was collected, 30-45-mesh particles was used for silanization. For immobilization about 10 mg CA in Tris or HEPES buffer pH 8.0 was used for immoblization per gram matrix. The inorganic support material is first treated with organo-functional silane as described elsewhere (Bunting and Laidler, 1972). The silane reacts with available oxide groups on the carrier surface leaving an organic functional group available for coupling to the enzyme. The reaction of the carrier, with gamma-aminopropyl-triethoxy-silane was used for coupling. Silane polymerizes across the surface of the carrier anchored at intervals (Bunting and Laidler, 1972; Kobayashi and Moo-Young, 1973). The amino derivative was covalently coupled using carbodiimides as described for other enzymes and matrices before (Chakrabarti et. al., 2003a) or converted into carboxyl derivative using alkylamine-carrier with succinic anhydride using published protocol for other enzymatic entities (Harhen and Barry, 1990). [0039] Preparation of glass coated cyanogens bromide activated carriers. A very thin layer of glass was coated on iron filings (40-60-mesh) and this thin layer of glass (Silicosteel; Restek) was used for direct attachment of carbonic anhydrase using cyanogen bromide mediated coupling (Srinivasan and Bumm, 1974; Chickere, et. al., 2001). About 10 mg CA in HEPES Buffer pH 8.0 was applied per gram of matrix for immobilization. [0040] Determination of mechanical stability of the immobilization matrix. The particle size distribution of controlled pore inert matrices were measured as a function of applied load to a standard volume of materials in a punch and die set within a pressure range 50 to 200 and 200 to 2500 psi (Eaton, 1974; Eaton 1976). Mercury intrusion porosimetry utilizing an Aminco-Winslow Porosimeter (Messing, 1970; Messing, 1974) was used to determine pore density of the immobilized porous materials. For this purpose both BSA and CA II was immobilized using all four methods and operated under pressures 50 to 200 and 200-2500 psi and the average pore diameter was estimated to determine breakage of matrix. [0041] Measurement of Pressure and Carbon dioxide in the emission gas. The pressure of the emission stream in the inlet and outlet was measured using HD8804 K pressure and temperature kit equipped with appropriate pressure probes. Some measurements were also made using Testo 525 instrument (Hotek Technologies, Tacoma Wash.). 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