Formulation and process for CO2 capture using amino acids and biocatalysts
A biocatalyst, amino acid technology, applied in the field of CO2 capture, can solve the problems of low ionic strength, not biodegradable, protein stability and unfavorable function
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Embodiment 1
[0082] Experiments were carried out in an absorption packed column. The absorption solution is an aqueous solution of potassium taurate (1,5M). The absorption solution and CO 2 The gas phase was contacted in countercurrent at a concentration of 130,000 ppm. The liquid flow rate was 0.65 g / min and the gas flow rate was 65 g / min, corresponding to a L / G of 10 (g / g). The gas and absorbing solution are at room temperature. The operating pressure of the absorber was set at 1.4 psig. The tower has a diameter of 7.5 cm and a height of 50 cm. The packing is 0.25 inch polymeric Raschig rings. Two tests were carried out: the first without biocatalyst and the second with carbonic anhydrase immobilized to the packing support.
[0083] The obtained results show that with carbonic anhydrase immobilized on the surface of Raschig rings, CO 2 transfer rate or CO 2 Increased removal rate from 83 to 117mmol CO 2 / minute. These results clearly demonstrate the positive effect of adding en...
Embodiment 2
[0085] The test was carried out in a stirred cell at an enzyme concentration of 500 mg / L in solutions of potassium glycinate (or the potassium salt of glycine) at concentrations of 0.1, 0.25 and 0.5 M and at a temperature of 20°C. The enzyme used was human carbonic anhydrase II (HCAII). initial CO 2 The loading is 0 mol / mol. The stirred tank contains the absorption solution (and enzymes, when required). Pure CO 2 A continuous stream of 1.0 is swept over the liquid phase in the stirred tank, and the pH change of the solution is monitored. Correlates changes in pH to changes in inorganic carbon concentration, which is used to calculate CO 2 transfer rate. The tests were carried out with and without enzymes to be able to determine the effect of the enzymes. Results are expressed as CO with enzyme 2 Transfer rate versus CO in the absence of enzyme 2 ratio of transfer rates (see image 3 ). The results clearly show that for K 2 CO 3 In all tests of the solutions, the en...
Embodiment 3
[0088] The tests were carried out in a stirred cell at an enzyme concentration of 500 mg / L in potassium methionine solutions (potassium salt of L-methionine) at concentrations of 0.1 and 0.25 M and at a temperature of 20°C. The enzyme used was human carbonic anhydrase II (HCAII). initial CO 2 The loading is 0 mol / mol. The stirred tank contains the absorption solution (and enzymes, when required). Pure CO 2 A continuous stream of 1.0 is swept over the liquid phase in the stirred tank, and the pH change of the solution is monitored. Correlates changes in pH to changes in inorganic carbon concentration, which is used to calculate CO 2 transfer rate. The tests were carried out with and without enzymes to be able to determine the effect of the enzymes. Results are expressed as CO with enzyme 2 Transfer rate versus CO in the absence of enzyme 2 Scale of transfer rates (see Table 1). The results clearly show that for all tests tested with potassium methionine solution, the e...
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