Abstract: Recombinant carbonic anhydrase variants having improved solubility and/or thermostability for enzyme-enhanced CO2 capture are provided. Host cells, methods, and processes relating to same are also provided.

Abstract: A method for stripping CO2 from a biocatalyst-containing CO2-rich absorption solution to produce a biocatalyst-containing CO2-lean absorption solution and a CO2-rich gas is provided. The method includes generating a stripping gas from a portion of the biocatalyst-containing CO2-lean absorption solution in a stripping gas generation unit, and contacting the biocatalyst-containing CO2-rich absorption solution with the stripping gas in a gas-liquid contactor to produce the CO2-lean absorption solution and the CO2-rich gas.

Abstract: Methods for enzyme-enhanced CO2 capture include contacting a CO2-containing gas with an aqueous absorption solution at process conditions—such as high temperature, high pH, and/or using carbonate-based solutions—in the presence of Thermovibrio ammonificans carbonic anhydrase (TACA) or functional derivative thereof for catalyzing the hydration reaction of CO2 into bicarbonate and hydrogen ions and/or catalyzing the desorption reaction to produce a CO2 gas. The TACA may be provided to flow with the solution to cycle through a CO2 capture system that includes an absorber and a stripper.

Abstract: The present description relates to recombinant or engineered carbonic anhydrase polypeptides, variants, and functional derivatives thereof, having improved properties that make them advantageous for use in CO2 capture operations (e.g., CO2 capture solvents, alkaline pH, and/or elevated temperatures), as well as polynucleotides and vectors encoding same. The present description also relates to methods, processes and systems for CO2 capture which make use of the recombinant or engineered carbonic anhydrase polypeptides, variants, and functional derivatives thereof.

Abstract: The present description relates to recombinant or engineered carbonic anhydrase polypeptides, variants, and functional derivatives thereof, having improved properties that make them advantageous for use in CO2 capture operations (e.g., CO2 capture solvents, alkaline pH, and/or elevated temperatures), as well as polynucleotides and vectors encoding same. The present description also relates to methods, processes and systems for CO2 capture which make use of the recombinant or engineered carbonic anhydrase polypeptides, variants, and functional derivatives thereof.

Abstract: Sulfurihydrogenibium sp. carbonic anhydrase (SspCA) or mutants thereof catalyze a hydration reaction of CO2 into bicarbonate and hydrogen ions or a desorption reaction to produce a CO2 gas. Sulfurihydrogenibium sp. carbonic anhydrase (SspCA) having improved thermostability in the presence of carbonate ions as compared to in the absence of carbonate ions are useful in the capture of CO2 from a CO2-containing gas.

Abstract: Methods for enzyme-enhanced CO2 capture include contacting a CO2-containing gas with an aqueous absorption solution at process conditions—such as high temperature, high pH, and/or using carbonate-based solutions—in the presence of Thermovibrio ammonificans carbonic anhydrase (TACA) or functional derivative thereof for catalyzing the hydration reaction of CO2 into bicarbonate and hydrogen ions and/or catalyzing the desorption reaction to produce a CO2 gas. The TACA may be provided to flow with the solution to cycle through a CO2 capture system that includes an absorber and a stripper.

Abstract: Use of Sulfurihydrogenibium sp. carbonic anhydrase (SspCA) or mutants thereof for catalyzing the hydration reaction of CO2 into bicarbonate and hydrogen ions or catalyzing the desorption reaction to produce a CO2 gas is provided.

Abstract: A method for CO2 capture may include operating a packed reactor comprising a reaction chamber containing packing including immobilized enzymes, by contacting a CO2 containing gas with a liquid solution in the reaction chamber to produce an ion-loaded solution and a CO2 depleted gas by an enzymatically catalyzed hydration reaction; monitoring enzyme activity of the immobilized enzymes; at a low enzyme activity threshold (i) stopping operation in the packed reactor, and (ii) replenishing the enzymatic activity by providing an enzyme replenishing solution into the packed reactor to contact the packing and provide a replenishing amount of the immobilized enzymes; and recommencing operation in the packed reactor for CO2 capture using the replenished immobilized enzymes. A corresponding system may include a packed reactor and an in situ enzyme supply device for supplying active enzyme within the reactor. The enzyme supply device may include spray nozzles with various configurations.

Abstract: Use of Sulfurihydrogenibium sp. carbonic anhydrase (SspCA) or mutants thereof for catalyzing the hydration reaction of CO2 into bicarbonate and hydrogen ions or catalyzing the desorption reaction to produce a CO2 gas is provided.

Abstract: A method for CO2 capture may include operating a packed reactor comprising a reaction chamber containing packing including immobilized enzymes, by contacting a CO2 containing gas with a liquid solution in the reaction chamber to produce an ion-loaded solution and a CO2 depleted gas by an enzymatically catalyzed hydration reaction; monitoring enzyme activity of the immobilized enzymes; at a low enzyme activity threshold (i) stopping operation in the packed reactor, and (ii) replenishing the enzymatic activity by providing an enzyme replenishing solution into the packed reactor to contact the packing and provide a replenishing amount of the immobilized enzymes; and recommencing operation in the packed reactor for CO2 capture using the replenished immobilized enzymes. A corresponding system may include a packed reactor and an in situ enzyme supply device for supplying active enzyme within the reactor. The enzyme supply device may include spray nozzles with various configurations.

Abstract: A method, process, apparatus, use and formulation for dual biocatalytic conversion of CO2 containing gas into carbon containing bio-products by enzymatic hydration of CO2 into bicarbonate ions in the presence of carbonic anhydrase and metabolic conversion of the bicarbonate ions into carbon containing bio-products in a biological culture. The dual biocatalytic conversion may be relatively constant with controlling a feeding of the bicarbonate ions to the biological culture in accordance with demands of the biological culture by retaining over-production of bicarbonate ions and feeding part of the over-production to the biological culture in accordance with nutrient demands of the biological culture. Bicarbonate ions may also be reconverted to generate a pure CO2 gas stream. The CO2 containing gas may be derived from operations of a power plant which receives a carbon-containing fuel for combustion, and the biological culture may be an algae culture.

Abstract: Techniques related to enhancement of CO2 absorption use selection of an enzyme coordinated with selection of an absorption solution having a pKa to enhance or maximize the CO2 capture rate. The techniques may use various relationships between process variables such as temperature, concentration, and so on, in order to provide efficient CO2 capture.

Abstract: AKR1B1 (EC 1.1.1.21) is an aldose reductase that has mainly been associated with the polyol pathway, and more recently with lipid deperoxidation. We have discovered that the primary activity of this enzyme is rather a PGFS activity, catalyzing the transformation of PGH2 into PGF2?. AKR1B1 as a therapeutic target, and method for modulating its expression and activity are provided. Methods for regulating the expression and activity of PGF2? are also provided.

Abstract: AKR1B1 (EC 1.1.1.21) is an aldose reductase that has mainly been associated with the polyol pathway, and more recently with lipid deperoxidation. We have discovered that the primary activity of this enzyme is rather a PGFS activity, catalyzing the transformation of PGH2 into PGF2?. AKR1B1 as a therapeutic target, and method for modulating its expression and activity are provided. Methods for regulating the expression and activity of PGF2? are also provided.