Polypeptides having carbonic anhydrase activity and polynucleotides encoding same

Abstract

The present invention relates to polypeptides having carbonic anhydrase activity and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.

Description

Reference to a Sequence Listing This application contains a Sequence Listing in computer readable form, which is incorporated herein by reference. Background of the Invention Field of the Invention The present invention relates to polypeptides having carbonic anhydrase activity, polynucleotides encoding the polypeptides, nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. The invention also relates to using the carbonic anhydrases in bioreactors for extracting carbon dioxide and compositions useful for such extraction processes. Description of the Related Art Carbon dioxide (CO2) emissions are a major contributor to the phenomenon of global warming. CO2 is a by-product of combustion and it creates operational, economic, and environmental problems. CO2 emissions may be controlled by capturing CO2 gas before emitted into the atmosphere. There are several chemical approaches to control the CO2 emissions (A. Kohl and R. Nielsen, Gas Purification, 5th ed., Gulf Professional Publishing, Houston, TX, 1997). However, many of these approaches have drawbacks such as high energy consumption, slow processes, and use of ecologically questionable or toxic compounds. An enzyme-based approach using the capability of carbonic anhydrase to catalyse the conversion of CO2 to bicarbonate at a very high rate (turnover is up to 106 molecules of CO2 per second), overcomes the reaction rates and environmental issues in relation to CO2 capture. Technical solutions for extracting CO2 from gases, such as combustion gases or respiration gases, using carbonic anhydrases have been described in WO 2006 / 089423, US 6,524,842, WO 2004 / 007058, WO 2004 / 028667, US 2004 / 0029257, US 7,132,090, WO 2005 / 114417, US 6,143,556, WO 2004 / 104160, US 2005 / 0214936, WO 2008 / 095057. Generally, these techniques operate by bringing a soluble or immobilized carbonic anhydrase into contact with CO2 which either may be in a gas phase or a liquid phase. In the presence of water, carbonic anhydrase catalyses the conversion of CO2 into bicarbonate ions which may be further protonated or deprotonated to carbonic acid and / or carbonate ions depending on the pH of the medium. The ions may either be utilized to facilitate growth of algae or microorganisms that utilize bicarbonate / carbonate as a carbon source, to induce a pH change in a surrounding medium or supply buffering capacity, to provide bicarbonate / carbonate as an active agent for subsequent chemical processes, or precipitated as a carbonate salt, or converted back into pure CO2, which can then be used (for example in enhanced oil recovery, for production of urea, for food and beverage processing, or to supply CO2 to greenhouses or cultivation ponds), released (for example from a contained life support environment such as a submarine, spacecraft, or artificial lung), compressed (for example for transportation through pipelines), or stored (such as in geological or deep oceanic formations or saline aquifers). Mammalian, plant and prokaryotic carbonic anhydrases (alpha- and beta-class CAs) generally function at physiological temperatures (37 °C) or lower temperatures. The temperature of combustion gasses or the liquids into which they are dissolved may, however, easily exceed the temperature optimum for the carbonic anhydrase used to capture the CO2. One of the drawbacks of using enzyme-based solutions is that extensive cooling may be needed in CO2 extraction processes prior to contacting the CO2-containing gas / liquid with the carbonic anhydrase, and cooling is an energy consuming process. Consequently, there is a need for more heat-stable carbonic anhydrases when the enzyme is to be used under industrially relevant conditions. A carbonic anhydrase obtainable from Persephonella marina is described in WO2012 / 025577. A metagenomic carbonic anhydrase isolated from the Logatchev hydrothermal is described in WO2018 / 017792. Variants of these enzymes with improved thermostability are described in PCT / US2023 / 081794. The present invention provides new carbonic anhydrase enzymes useful for CO2 capture. Summary of the Invention The present invention provides polypeptides having carbonic anhydrase activity and polynucleotides encoding the polypeptides. Accordingly, the present invention relates to polypeptides having carbonic anhydrase activity selected from the group consisting of: (a) a polypeptide having at least 60% sequence identity to any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 79, 81, 83, and 85; (b) a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of any one of SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 78, 80, 82, and 84; (c) a polypeptide derived from any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 79, 81, 83, and 85 by having 1-30 alterations (e.g., substitutions, deletions and / or insertions at one or more positions, e.g., 1 or 2 or 3 or 4 or 5 or 6 or 7 or 8 or 9 or 10 or 11 or 12 or 13 or 14 or 15 or 16 or 17 or 18 or 19 or 20 or 21 or 22 or 23 or 24 or 25 or 26 or 27 or 28 or 29 or 30 alterations, in particular substitutions; (d) a polypeptide having a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 79, 81, 83, and 85, wherein the three-dimensional structure is calculated by Alphafold. (e) a polypeptide derived from the polypeptide of (a), (b), (c) or (d) wherein the N-and / or C-terminal end has been extended by addition of one or more amino acids; and (f) a fragment of the polypeptide of (a), (b), (c) or (d); wherein the polypeptide has carbonic anhydrase activity. The present invention also relates to polynucleotides encoding the polypeptides of the present invention; nucleic acid constructs; recombinant expression vectors; recombinant host cells comprising the polynucleotides; and methods of producing the polypeptides. The present invention also relates to methods of of using the carbonic anhydrases for extraction of carbon dioxide from a carbon dioxide-containing medium. Brief Description of the Figures Figure 1 shows a schematic diagram of a counter-current gas-liquid contactor. In a typical counter-current gas-liquid contactor, the CO2-rich inlet gas (e.g., a mixed gas comprising CO2) enters the bottom of the contactor and travels upwards, while the CO2-lean inlet liquid enters the top of the contactor and flows downwards. The liquid flow can be in the form of droplets, such as a spray, or as a continuous stream or sheet of liquid, such as flows along a surface, or a combination of these. Inside the gas-liquid contactor, CO2 from the CO2-rich inlet gas is absorbed by the liquid and carried out from the contactor as a CO2-rich outlet liquid. CO2-rich liquid means the liquid comprises an increased amount of CO2 in its dissolved gaseous form or any ionic form of CO2, such as bicarbonate, or a reaction product of CO2 and a compound in the inlet absorption liquid, relative to the CO2-lean liquid. CO2-lean gas, from which CO2 has been partially or completely removed, exits the contactor as the outlet gas. A counter-current gas-liquid contactor is the most common type of gas-liquid contactor used industrially. The internals of the contactor can be largely empty with liquid sprayed down from the top and gas flowing up from the bottom, or, more commonly, the contactor contains different types of packing materials to increase the residence time of gas and liquid inside the contactor and promote a large surface area of interaction between the gas and liquid. The liquid is typically delivered onto the packing materials from spray nozzles or other types of openings designed to deliver the liquid in a uniform fashion over the packing material. The liquid is comprised of absorption compounds, water, and other components that may be needed to optimize the process. For example, the liquid can comprise CA in soluble form or as small particles of suspended biocatalyst that flow through the contactor. The packing material may be coated with or have CA attached to it. Figure 2 shows a schematic diagram of a co-current gas-liquid contactor. In a typical cocurrent gas-liquid contactor, the CO2-rich inlet gas and CO2-lean inlet liquid enter the contactor at the same end (e.g., the top) and exit at the same end. The outlet gas preferably exits the contactor at a location above any sump present for collection of the outlet liquid. This type of contactor can provide a lower pressure drop compared to a counter-current contactor, because the gas and liquid flows are both moving in the same direction, however the efficiency of gasliquid interaction may be lower compared to a counter-current design. The internals and function of the co-current contactor are as described for Figure 1, with the exception that the gas and liquid are flowing in the same direction. Figure 3 shows a schematic diagram of a perpendicular-flow gas-liquid contactor. In a perpendicular gas-liquid contactor, the gas typically travels in an overall horizontal direction from the inlet gas to the outlet gas while the liquid overall travels vertically, from inlet liquid at the top to outlet liquid at the bottom to take advantage of gravity. This contactor design can take advantage of specialized liquid delivery systems, such as those generating flat sheets of liquid, to create high gas-liquid contact in a compact design that does not require tall vertical structures. The contactor can have internal baffles or packing materials to enhance gas-liquid contact and control gas and liquid flows. The internals and function of the co-current contactor are as described for Figure 1, with the exception that the overall gas and liquid flows are perpendicular to each other. Figure 4 shows a schematic diagram of a membrane gas-liquid contactor. A membrane contactor utilizes a gas permeable membrane (dotted line) to separate the gas flow from the liquid flow. The diagram shows counter-current flow of gas and liquid, though co-current and perpendicular-type flows are also possible. The CO2-rich inlet gas comes in contact with the membrane and CO2, preferably selectively, passes across the membrane into the CO2 absorption liquid. Membranes used in these contactors can be microporous, allowing the surface of the liquid to be exposed to the gas through pores in the membrane that are small enough to prevent the liquid from passing through due to physical phenomena, such as surface tension. Alternatively, the membranes can be non-porous, yet made from CO2-gas permeable materials. Microporous membranes may provide faster CO2 absorption rates, while non-porous membranes may minimize liquid losses to evaporation in the gas stream. While passing through the contactor, the inlet liquid becomes enriched in CO2, such that the outlet liquid is CO2-rich by comparison, and the inlet gas becomes depleted in CO2, such that the outlet gas is CO2-lean. The diagram only shows a representation of the basic functional unit of a membrane contactor, which in operational form contains many layers of stacked membranes or bundles of tubular, or hollow-fiber, membranes arranged in suitable housing with dividers and control mechanisms to optimally direct the gas and liquid flows. Membrane contactors are used for large industrial gas scrubbing applications as well as for small units, such as for CO2 removal during dialysis in which the semi-permeable membrane may separate two liquids, such as CO2-rich blood and a CO2-lean buffer solution capable of absorbing excess CO2 from the blood. CA can be present in soluble or suspended particulate form in the liquid and can be immobilized on or in the membrane. Figure 5 shows a schematic diagram of a bubble-tank gas-liquid contactor. The system shown is a batch-mode bubble-tank gas-liquid contactor, in which a stream of inlet gas comprising CO2 is bubbled (or sparged) through a fixed amount of absorption liquid. CO2 is absorbed into the liquid such that the outlet gas is depleted in CO2 compared to the inlet gas. In batch mode, eventually the liquid will reach a maximum CO2 absorption capacity, and the CO2-rich inlet gas can be directed to another batch reactor containing CO2-lean absorption liquid, or the batch reactor can be emptied and filled with fresh CO2-lean absorption liquid, or the inlet gas flow can be stopped while the batch reactor is changed from absorption mode to CO2 desorption mode, such as by applying heat, sweep gas or vacuum to the batch reactor, to release absorbed CO2 from the CO2-rich liquid. This type of contactor can, for example, be used for producing solid precipitated forms of CO2, such as carbonates, like calcium, magnesium, and manganese carbonate. Gas delivery nozzles that produce very small gas bubbles can enhance the gas-liquid contact and improve CO2 absorption efficiency. A bubble-tank contactor can be enclosed equipment or can operate in open environments, such as bubbling CO2-rich gas streams into algae ponds. CA can be present in soluble or suspended particulate form in the liquid and can be immobilized on the surfaces of structures or packing immersed in or exposed to the liquid. Figure 6 shows a schematic diagram of a batch-mode stirred-tank gas-liquid contactor. In this type of contactor, the CO2-rich gas is exposed to the surface of a liquid leading to CO2 gas absorption into the liquid. The liquid may be quiescent or may be mixed by some means to cause movement of the liquid and liquid components. The principle of a stirred-tank contactor can apply to controlled enclosed equipment or can apply to open environments, such the absorption of CO2 from air into a body of water, like an ocean. CA can be present in soluble or suspended particulate form in the liquid and can be immobilized on the surfaces of structures, mixers or packing immersed in or exposed to the liquid. Figure 7 shows a schematic diagram of an integrated CO2 scrubbing system. In the system shown, CO2-rich feed gas (1) enters near the bottom of the absorber (2) and flows upwards where it comes in contact with CO2-lean absorption liquid (3) that enters the absorber near the top. Scrubbed gas (4), from which CO2 has been removed, exits the absorber at the top. CO2-rich absorption liquid (5) exits at the bottom of the absorber and (optionally) passes through a biocatalyst recovery unit (6) which separates the catalyst for recycling (7) and redelivery into the absorber along with the CO2-lean absorption liquid (3). The main amount of CO2-rich absorption liquid (5) exits the (optional) biocatalyst recovery unit (6) and travels to an optional temperature regulator (e.g., heat exchanger) (8) where the CO2-rich absorption liquid is pre heated before traveling to the desorber (9). The CO2-rich absorption liquid enters near the top of the desorber and flows downwards. Heat is supplied to the desorber by any suitable means, e.g., a re-boiler, and optionally another desorption driving force such as a sweep gas (10) or vacuum (13), or a combination of these applied to the desorber causing extracted CO2 to be released from the absorption liquid and exit the desorber, (optionally) passing through an absorption liquid condenser (11) to remove absorption liquid vapor from the gas stream, and (optionally) passing through a sweep gas condenser (12) to remove sweep gas compounds from the CO2 gas stream prior to release, compression and / or use of the purified CO2 gas (14). Sweep gas compounds separated in the sweep gas condenser (12) are optionally recycled and fed back to the desorber along with the provision of fresh sweep gas (10). CO2- lean absorption liquid (15) exits the desorber, and (optionally) passes through a second biocatalyst recovery unit (16), which separates the biocatalyst for recycling (17) and redelivery into the desorber along with the CO2-rich absorption liquid (5), before (optionally) passing through a temperature regulator (8), and (optionally) passing through a secondary CO2 desorber (18) before returning to the absorber (3). Although the secondary CO2 desorber may function by any of the known means of desorption, a preferred mode of operation for the secondary CO2 desorber is as a secondary air sweep desorber utilizing a membrane-based design, in which CO2-lean sweep gas (22), such as air is contacted with the CO2-lean liquid (15) to further remove residual CO2 remaining in the CO2-lean liquid (15) and provide a very CO2-lean liquid (3) for re-entry to the absorber. The secondary sweep gas (23) exiting the secondary CO2 desorber (18) can be released to the atmosphere or can be used for a purpose, such as to supply air for combustion, e.g., when the CO2 scrubber is installed at a power plant. Depleted biocatalyst and / or other depleted components of the absorption liquid can be added at various points in the process, such as at the locations indicated (20 and 21). Removal of samples for process monitoring and control of liquid levels as well as removal of insoluble contaminants can be carried out at various points in the process, such as at the locations indicated (24 and 25). Although not depicted in the diagram, it is understood that pumps to provide and control liquid flow, blowers to provide and control gas flow, and all relevant valves, meters, instrumentation and equipment for process control and monitoring can be installed and utilized at the needed locations. CA can be present in soluble or suspended particulate form in the liquid as it flows through the system and can be immobilized on the surfaces of structures, mixers or packing material immersed in or exposed to the liquid. Figure 8 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the Endozoicomonas arenosclerae carbonic anhydrase of SEQ ID NO: 2 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 9 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the Achromatium sp. carbonic anhydrase of SEQ ID NO: 4 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 10 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the Endozoicomonas numazuensis carbonic anhydrase of SEQ ID NO: 6 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 11 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the Thiorhodococcus drewsii carbonic anhydrase of SEQ ID NO: 8 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 12 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 10 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 13 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 12 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 14 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the Aquificales bacterium carbonic anhydrase of SEQ ID NO: 14 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 15 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 16 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 16 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 18 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 17 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 20 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 18 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 22 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 19 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 26 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 20 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 28 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 21 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 30 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 22 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 32 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 23 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 34 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 24 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 36 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 25 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 38 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 26 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 40 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 27 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 42 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 28 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 44 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 29 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 46 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 30 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 48 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 31 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 50 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 32 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 52 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 33 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 54 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 34 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 56 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 35 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 58 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 36 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 60 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 37 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 62 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 38 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 64 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 39 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 66 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 40 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 68 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 41 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 70 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 42 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the Trichophaea saccata carbonic anhydrase of SEQ ID NO: 74 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 43 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the Eleutherascus tuberculatus carbonic anhydrase of SEQ ID NO: 76 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 44 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the Lactobacillus sp. carbonic anhydrase of SEQ ID NO: 79 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 45 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 81 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 46 is a sequence alignment of the Persephonella marina carbonic anhydrase of SEQ ID NO: 77 (top) with the carbonic anhydrase of SEQ ID NO: 83 (bottom). Key residues described herein that may be important for activity are indicated with the * symbol. Figure 47 shows the normalized WAU activity of carbonic anhydrases relative to the Persophenella marina carbonic anhydrase as described in Example 3. Figure 48 shows the normalized WAU activity of carbonic anhydrases relative to the Persophenella marina carbonic anhydrase as described in Example 4. Definitions In accordance with this detailed description, the following definitions apply. Note that the singular forms "a," "an," and "the" include plural references unless the context clearly dictates otherwise. Unless defined otherwise or clearly indicated by context, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Carbonic anhydrase: The term “carbonic anhydrase” means an enzyme of EC 4.2.1.1 having carbonic anhydrase activity. Carbonic anhydrase Activity: The term “carbonic anhydrase activity” or “CA activity” is defined herein as an EC 4.2.1.1 activity which catalyzes the conversion between carbon dioxide and bicarbonate [CO2 + H2O HCOa' + H+], For purposes of the present invention, CA activity may be determined according to the procedure described in WO2018 / 017792 (the content of which is incorporated herein by reference). One unit of CA activity is defined after Wilbur [1 U = (1 / tc)-(1 / tu) x 1000] where U is units and tc and tu represent the time in seconds for the catalyzed and uncatalyzed reaction, respectively (Wilbur, 1948, J. Biol. Chern. 176: 147-154). cDNA: The term "cDNA" means a DNA molecule that can be prepared by reverse transcription from a mature, spliced, mRNA molecule obtained from a eukaryotic or prokaryotic cell. cDNA lacks intron sequences that may be present in the corresponding genomic DNA. The initial, primary RNA transcript is a precursor to mRNA that is processed through a series of steps, including splicing, before appearing as mature spliced mRNA. CO2-lean / CO2-rich: The terms “CO2-lean” and “CO2-rich” carrier liquid are terms used in the present invention to describe the relative amount of carbon (e.g., in the form of dissolved CO2, chemically reacted CO2, bicarbonate, carbonic acid and / or carbonate salt) present in the carrier liquid as it circulates through the process. As used herein, the term “CO2-lean carrier liquid” generally refers to carrier liquid entering an absorption module. The term “CO2-rich carrier liquid” generally refers to a carrier liquid entering a desorption module. It is understood that the term 10 “C02-lean carrier liquid” can also be applied to carrier liquid exiting a desorption module, and the term “C02-rich carrier liquid” can also be applied to carrier liquid exiting an absorption module. C02-rich carrier liquid contains more carbon compared to CO2-lean carrier liquid within a system at a given point in time. CO2-containing medium: The term “CO2-containing medium” is used to describe any material which contains at least 0.001% CO2, preferably at least 0.01%, more preferably at least 0.1%, more preferably at least 1%, more preferably at least 5%, most preferably 10%, even more preferred at least 20%, and even most preferably at least 50% CO2. Preferably the CO2-containing medium has a temperature between 5 °C and 110 °C, more preferably between 10 °C and 100 °C, more preferably between 20 °C and 95 °C, more preferably between 30 °C and 90 °C, more preferably between 40 °C and 85 °C, more preferably between 50 °C and 80 °C, more preferably between 55 °C and 75 °C and most preferably between 60 °C and 70 °C at any pressure. CO2-containing media are in particular gaseous phases (including gas mixtures), liquids or multiphase mixtures, but may also be solid. A CO2-containing gaseous phase is for example raw natural gas obtainable from oil wells, gas wells, and condensate wells, syngas generated by the gasification of a carbon containing fuel (e.g., methane) to a gaseous product comprising CO and H2, or emission streams from combustion processes, e.g., from carbon based electric generation power plants, or from flue gas stacks from such plants, industrial furnaces, stoves, ovens, or fireplaces or from airplane or car exhausts. A CO2-containing gaseous phase may alternatively be ambient air (including hot (above 40°C) air, e.g., desert air), or from respiratory processes in mammals (such as the CO2-containing gas phase in an artificial lung), living plants and other CO2 emitting species, in particular from green-houses. A CO2-containing gas phase may also be off-gas, from aerobic or anaerobic fermentation, such as brewing, fermentation to produce useful products such as ethanol, or the production of biogas. Such fermentation processes can occur at elevated temperatures if they are facilitated by thermophilic microorganisms, which are for example encountered in the production of biogas. A CO2-containing gaseous phase may alternatively be a gaseous phase enriched in CO2 for the purpose of use or storage. The above-described gaseous phases may also occur as multiphase mixtures, where the gas co-exists with a certain degree of fluids (e.g., water or other solvents) and / or solid materials (e.g., ash or other particles). CO2-containing liquids are any solution or fluid, in particular aqueous liquids, containing measurable amounts of CO2, preferably at one of the levels mentioned above at any pressure. CO2-containing liquids may be obtained by passing a CO2-containing gas or solid (e.g., dry ice or soluble carbonate containing salt) into the liquid. CO2-containing fluids may also be compressed CO2 liquid (that contains contaminants, such as drycleaning fluid), supercritical CO2, orCO2 solvent liquids, like ionic liquids. A CO2-containing liquid may also be referred to as a “carrier liquid”. A CO2-containing liquid may also include compounds capable of improving the CO2-containing capacity of the liquid, such as HCO3' (KHCO3 or NaHCO3), CO32' (Na2CO3 or K2CO3), HPO42' (K2HPO4 or Na2HPO4) or MDEA or Tris. CO2 extraction: The term “CO2 extraction” is to be understood as a reduction of carbon from a CO2-containing medium. Such an extraction may be performed from one medium to another, e.g., gas to liquid, liquid to gas, gas to liquid to gas, liquid to liquid or liquid to solid, but the extraction may also be the conversion of CO2 to bicarbonate, carbonate or carbonic acid within the same medium or the conversion of bicarbonate to CO2 within the same medium. The term CO2 capture is also used to indicate extraction of CO2 from one medium to another or conversion of CO2 to bicarbonate / carbonate or conversion of bicarbonate / carbonate to CO2. Coding sequence: The term “coding sequence” means a polynucleotide, which directly specifies the amino acid sequence of a polypeptide. The boundaries of the coding sequence are generally determined by an open reading frame, which begins with a start codon, such as ATG, GTG, or TTG, and ends with a stop codon, such as TAA, TAG, or TGA. The coding sequence may be a genomic DNA, cDNA, synthetic DNA, or a combination thereof. Control sequences: The term “control sequences” means nucleic acid sequences involved in regulation of expression of a polynucleotide in a specific organism or in vitro. Each control sequence may be native (i.e., from the same gene) or heterologous (i.e., from a different gene) to the polynucleotide encoding the polypeptide, and native or heterologous to each other. Such control sequences include, but are not limited to leader, polyadenylation, prepropeptide, propeptide, signal peptide, promoter, terminator, enhancer, and transcription or translation initiator and terminator sequences. Ata minimum, the control sequences include a promoter, and transcriptional and translational stop signals. The control sequences may be provided with linkers for the purpose of introducing specific restriction sites facilitating ligation of the control sequences with the coding region of the polynucleotide encoding a polypeptide. Expression: The term “expression” means any step involved in the production of a polypeptide including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification, and secretion. Expression vector: An "expression vector" refers to a linear or circular DNA construct comprising a DNA sequence encoding a polypeptide, which coding sequence is operably linked to a suitable control sequence capable of effecting expression of the DNA in a suitable host. Such control sequences may include a promoter to effect transcription, an optional operator sequence to control transcription, a sequence encoding suitable ribosome binding sites on the mRNA, enhancers and sequences which control termination of transcription and translation. Extension: The term “extension” means an addition of one or more amino acids to the amino and / or carboxyl terminus of a polypeptide, wherein the “extended” polypeptide has carbonic anhydrase activity. Fragment: The term “fragment” means a polypeptide having one or more amino acids absent from the amino and / or carboxyl terminus of the mature polypeptide, wherein the fragment has carbonic anhydrase activity. Fusion polypeptide: The term “fusion polypeptide” is a polypeptide in which one polypeptide is fused at the N-terminus and / or the C-terminus of a polypeptide of the present invention. A fusion polypeptide is produced by fusing a polynucleotide encoding another polypeptide to a polynucleotide of the present invention, or by fusing two or more polynucleotides of the present invention together. Techniques for producing fusion polypeptides are known in the art, and include ligating the coding sequences encoding the polypeptides so that they are in frame and that expression of the fusion polypeptide is under control of the same promoter(s) and terminator. Fusion polypeptides may also be constructed using intein technology in which fusion polypeptides are created post-translationally (Cooper et al., 1993, EMBO J. 12: 2575-2583; Dawson et al., 1994, Science 266: 776-779). A fusion polypeptide can further comprise a cleavage site between the two polypeptides. Upon secretion of the fusion protein, the site is cleaved releasing the two polypeptides. Examples of cleavage sites include, but are not limited to, the sites disclosed in Martin et al., 2003, J. Ind. Microbiol. Biotechnol. 3: 568-576; Svetina et al., 2000, J. Biotechnol. 7Q: 245-251; Rasmussen-Wilson et al., 1997, Appl. Environ. Microbiol. 63: 3488-3493; Ward et al., 1995, Biotechnology 13: 498-503; and Contreras et al., 1991, Biotechnology 9: 378-381; Eaton et al., 1986, Biochemistry 25: 505-512; Collins-Racie et al., 1995, Biotechnology 13: 982-987; Carter etal., 1989, Proteins: Structure, Function, and Genetics 6: 240-248; and Stevens, 2003, Drug Discovery World 4: 35-48. Heat-stable: The term “heat-stable” or “thermostable” as used in reference to a carbonic anhydrase indicates that the enzyme is functional or active (i.e., can perform catalysis) at an elevated temperature, i.e., above 45°C, preferably above 50°C, more preferably above 55°C, more preferably above 60°C, even more preferably above 65°C, most preferably above 70°C, most preferably above 75°C, most preferably above 80°C, most preferably above 85°C most preferably above 90°C, and even most preferably above 100°C. In a preferred embodiment the carbonic anhydrase displays optimum activity at one of the temperatures indicated above, i.e., the enzyme’s temperature optimum is at one of the temperatures indicated above. The temperature stability of the carbonic anhydrase can be increased to some extent by way of formulation, e.g., by combination with stabilizing chemicals or by immobilization of the enzyme or by chemical modification, e.g., cross-linking, to preserve the enzyme in its active threedimensional shape. In order for an enzyme to be considered as heat-stable it remains active after at least 15 minutes, preferably for at least 2 hours, more preferably for at least 24 hours, more preferably for at least 7 days, more preferably for at least 10 days, even more preferably for at least 14 days, most preferably for at least 30 days, even most preferably for at least 50 days at the elevated temperature. The level of activity may be measured using an assay described in WO2018 / 017792, e.g., after incubation for the given time in 1 M NaHCOs buffer at pH 8 at the given elevated temperature. The activity may be compared with the enzyme activity prior to the temperature elevation, thereby obtaining the residual activity of the enzyme after the heat treatment. Preferably, the residual activity is at least 30% after the given time at the elevated 13 temperature, more preferably at least 40%, more preferably at least 50%, more at least 60%, even more preferably at least 70%, most preferably at least 80%, even most preferably the residual activity is at least 90%, and absolutely most preferred the level of residual activity is at least equal to or unchanged after the given time at the elevated temperature. Heterologous: The term "heterologous" means, with respect to a host cell, that a polypeptide or nucleic acid does not naturally occur in the host cell. The term "heterologous" means, with respect to a polypeptide or nucleic acid, that a control sequence, e.g., promoter, of a polypeptide or nucleic acid is not naturally associated with the polypeptide or nucleic acid, i.e., the control sequence is from a gene other than the gene encoding the mature polypeptide. Host Strain or Host Cell: A "host strain" or "host cell" is an organism into which an expression vector, phage, virus, or other DNA construct, including a polynucleotide encoding a polypeptide of interest (e.g., an amylase) has been introduced. Exemplary host strains are microorganism cells (e.g., bacteria, filamentous fungi, and yeast) capable of expressing the polypeptide of interest and / or fermenting saccharides. The term "host cell" includes protoplasts created from cells. Introduced: The term "introduced" in the context of inserting a nucleic acid sequence into a cell, means "transfection", "transformation" or "transduction," as known in the art. Isolated: The term “isolated” means a polypeptide, nucleic acid, cell, or other specified material or component that has been separated from at least one other material or component, including but not limited to, other proteins, nucleic acids, cells, etc. An isolated polypeptide, nucleic acid, cell or other material is thus in a form that does not occur in nature. An isolated polypeptide includes, but is not limited to, a culture broth containing the secreted polypeptide expressed in a host cell. Mature polypeptide: The term “mature polypeptide” means a polypeptide in its mature form following N-terminal processing and / or C-terminal processing (e.g., removal of signal peptide). Mature polypeptide coding sequence: The term “mature polypeptide coding sequence” means a polynucleotide that encodes a mature polypeptide having carbonic anhydrase activity. Native: The term "native" means a nucleic acid or polypeptide naturally occurring in a host cell. Nucleic acid: The term "nucleic acid" encompasses DNA, RNA, heteroduplexes, and synthetic molecules capable of encoding a polypeptide. Nucleic acids may be single stranded or double stranded and may be chemical modifications. The terms "nucleic acid" and "polynucleotide" are used interchangeably. Because the genetic code is degenerate, more than one codon may be used to encode a particular amino acid, and the present compositions and methods encompass nucleotide sequences that encode a particular amino acid sequence. Unless otherwise indicated, nucleic acid sequences are presented in 5'-to-3' orientation. Nucleic acid construct: The term "nucleic acid construct" means a nucleic acid molecule, either single- or double-stranded, which is isolated from a naturally occurring gene or is modified to contain segments of nucleic acids in a manner that would not otherwise exist in nature, or which is synthetic, and which comprises one or more control sequences operably linked to the nucleic acid sequence. Operably linked: The term "operably linked" means that specified components are in a relationship (including but not limited to juxtaposition) permitting them to function in an intended manner. For example, a regulatory sequence is operably linked to a coding sequence such that expression of the coding sequence is under control of the regulatory sequence. Purified: The term “purified” means a nucleic acid, polypeptide or cell that is substantially free from other components as determined by analytical techniques well known in the art (e.g., a purified polypeptide or nucleic acid may form a discrete band in an electrophoretic gel, chromatographic eluate, and / or a media subjected to density gradient centrifugation). A purified nucleic acid or polypeptide is at least about 50% pure, usually at least about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, about 99.5%, about 99.6%, about 99.7%, about 99.8% or more pure (e.g., percent by weight or on a molar basis). In a related sense, a composition is enriched for a molecule when there is a substantial increase in the concentration of the molecule after application of a purification or enrichment technique. The term "enriched" refers to a compound, polypeptide, cell, nucleic acid, amino acid, or other specified material or component that is present in a composition at a relative or absolute concentration that is higher than a starting composition. In one aspect, the term "purified" as used herein refers to the polypeptide or cell being essentially free from components (especially insoluble components) from the production organism. In other aspects, the term "purified" refers to the polypeptide being essentially free of insoluble components (especially insoluble components) from the native organism from which it is obtained. In one aspect, the polypeptide is separated from some of the soluble components of the organism and culture medium from which it is recovered. The polypeptide may be purified ( / .e., separated) by one or more of the unit operations filtration, precipitation, or chromatography. Accordingly, the polypeptide may be purified such that only minor amounts of other proteins, in particular, other polypeptides, are present. The term "purified" as used herein may refer to removal of other components, particularly other proteins and most particularly other enzymes present in the cell of origin of the polypeptide. The polypeptide may be "substantially pure", i.e., free from other components from the organism in which it is produced, e.g., a host organism for recombinantly produced polypeptide. In one aspect, the polypeptide is at least 40% pure by weight of the total polypeptide material present in the preparation. In one aspect, the polypeptide is at least 50%, 60%, 70%, 80% or 90% pure by weight of the total polypeptide material present in the preparation. As used herein, a "substantially pure polypeptide" may denote 15 a polypeptide preparation that contains at most 10%, preferably at most 8%, more preferably at most 6%, more preferably at most 5%, more preferably at most 4%, more preferably at most 3%, even more preferably at most 2%, most preferably at most 1%, and even most preferably at most 0.5% by weight of other polypeptide material with which the polypeptide is natively or recombinantly associated. It is, therefore, preferred that the substantially pure polypeptide is at least 92% pure, preferably at least 94% pure, more preferably at least 95% pure, more preferably at least 96% pure, more preferably at least 97% pure, more preferably at least 98% pure, even more preferably at least 99% pure, most preferably at least 99.5% pure by weight of the total polypeptide material present in the preparation. The polypeptide of the present invention is preferably in a substantially pure form ( / .e., the preparation is essentially free of other polypeptide material with which it is natively or recombinantly associated). This can be accomplished, for example by preparing the polypeptide by well-known recombinant methods or by classical purification methods. Recombinant: The term "recombinant" is used in its conventional meaning to refer to the manipulation, e.g., cutting and rejoining, of nucleic acid sequences to form constellations different from those found in nature. The term recombinant refers to a cell, nucleic acid, polypeptide or vector that has been modified from its native state. Thus, for example, recombinant cells express genes that are not found within the native (non-recombinant) form of the cell, or express native genes at different levels or under different conditions than found in nature. The term “recombinant” is synonymous with “genetically modified” and “transgenic”. Recover: The terms "recover" or “recovery” means the removal of a polypeptide from at least one fermentation broth component selected from the list of a cell, a nucleic acid, or other specified material, e.g., recovery of the polypeptide from the whole fermentation broth, or from the cell-free fermentation broth, by polypeptide crystal harvest, by filtration, e.g. depth filtration (by use of filter aids or packed filter medias, cloth filtration in chamber filters, rotary-drum filtration, drum filtration, rotary vacuum-drum filters, candle filters, horizontal leaf filters or similar, using sheed or pad filtration in framed or modular setups) or membrane filtration (using sheet filtration, module filtration, candle filtration, microfiltration, ultrafiltration in either cross flow, dynamic cross flow or dead end operation), or by centrifugation (using decanter centrifuges, disc stack centrifuges, hyrdo cyclones or similar), or by precipitating the polypeptide and using relevant solid-liquid separation methods to harvest the polypeptide from the broth media by use of classification separation by particle sizes. Recovery encompasses isolation and / or purification of the polypeptide. Secreted: The term “secreted” as used herein is to be understood as a polypeptide which after expression in a cell is either transported to and released to the surrounding extracellular medium or is associated / embedded in the cellular membrane so that at least a part of the polypeptide is exposed to the surrounding extracellular medium. Sequence identity: The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity”. For purposes of the present invention, the sequence identity between two amino acid sequences is determined as the output of “longest identity” using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 6.6.0 or later. The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. In order for the Needle program to report the longest identity, the -nobrief option must be specified in the command line. The output of Needle labeled “longest identity” is calculated as follows: (Identical Residues x 100) / (Length of Alignment-Total Number of Gaps in Alignment) For purposes of the present invention, the sequence identity between two polynucleotide sequences is determined as the output of “longest identity” using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), preferably version 6.6.0 or later. The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NLIC4.4) substitution matrix. In order for the Needle program to report the longest identity, the nobrief option must be specified in the command line. The output of Needle labeled “longest identity” is calculated as follows: (Identical Deoxyribonucleotides x 100) / (Length of Alignment - Total Number of Gaps in Alignment) Signal Peptide: A "signal peptide" is a sequence of amino acids attached to the N-terminal portion of a protein, which facilitates the secretion of the protein outside the cell. The mature form of an extracellular protein lacks the signal peptide, which is cleaved off during the secretion process. Subsequence: The term “subsequence” means a polynucleotide having one or more nucleotides absent from the 5' and / or 3' end of a mature polypeptide coding sequence; wherein the subsequence encodes a fragment having carbonic anhydrase activity. Syngas: The term “syngas” or “synthesis gas” is used to describe a gas mixture that contains varying amounts of carbon monoxide and hydrogen generated by the gasification of a carbon containing fuel (e.g., methane or natural gas) to a gaseous product with a heating value. CO2 is produced in the syngas reaction and must be removed to increase the heating value. Thermophilic: The term “thermophilic” in relation to an organism, describes an organism which thrives at relatively high temperatures, i.e., above 45 °C. Hyperthermophilic organisms thrive in extremely hot environments, that is, hotter than around 60 °C with an optimal temperature above 80 °C. Variant: The term “variant” means a polypeptide having carbonic anhydrase activity comprising a man-made mutation, i.e., a substitution, insertion (including extension), and / or deletion (e.g., truncation), at one or more positions. A substitution means replacement of the amino acid occupying a position with a different amino acid; a deletion means removal of the amino acid occupying a position; and an insertion means adding 1-5 amino acids (e.g., 1-3 amino acids, in particular, 1 amino acid) adjacent to and immediately following the amino acid occupying a position. Wild-type: The term "wild-type" in reference to an amino acid sequence or nucleic acid sequence means that the amino acid sequence or nucleic acid sequence is a native or naturally-occurring sequence. As used herein, the term "naturally-occurring" refers to anything (e.g., proteins, amino acids, or nucleic acid sequences) that is found in nature. Conversely, the term "non-naturally occurring" refers to anything that is not found in nature (e.g., recombinant nucleic acids and protein sequences produced in the laboratory or modification of the wild-type sequence). Detailed Description of the Invention Polypeptides Having Carbonic Anhydrase Activity The present invention relates to polypeptides having carbonic anhydrase activity. In one aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 2; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 1; (c) a polypeptide derived from or SEQ ID NO: 2 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 2. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 2. The polypeptide of any of the embodiments above related to SEQ ID NO: 2 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 2. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 1. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 1. In another embodiment, the polypeptide is derived from SEQ ID NO: 2 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 2 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 2 is up to 15, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 4; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 3; (c) a polypeptide derived from or SEQ ID NO: 4 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 4. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 4. The polypeptide of any of the embodiments above related to SEQ ID NO: 4 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 4. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 3. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 3. In another embodiment, the polypeptide is derived from SEQ ID NO: 4 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 4 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 4 is up to 15, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 6; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 5; (c) a polypeptide derived from or SEQ ID NO: 6 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 6. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 6. The polypeptide of any of the embodiments above related to SEQ ID NO: 6 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 6. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 5. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 5. In another embodiment, the polypeptide is derived from SEQ ID NO: 6 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 6 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 6 is up to 15, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 8; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 7; (c) a polypeptide derived from or SEQ ID NO: 8 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 8. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 8. The polypeptide of any of the embodiments above related to SEQ ID NO: 8 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 8. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, 21 at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 7. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 7. In another embodiment, the polypeptide is derived from SEQ ID NO: 8 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 8 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 8 is upto 15, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 10; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 9; (c) a polypeptide derived from or SEQ ID NO: 10 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 10. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 10. The polypeptide of any of the embodiments above related to SEQ ID NO: 10 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 10. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, 22 at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 9. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 9. In another embodiment, the polypeptide is derived from SEQ ID NO: 10 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 10 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 10 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 12; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 11; (c) a polypeptide derived from or SEQ ID NO: 12 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 12. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 12. The polypeptide of any of the embodiments above related to SEQ ID NO: 12 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 12. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 11. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 11. In another embodiment, the polypeptide is derived from SEQ ID NO: 12 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 12 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 12 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 14; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 13; (c) a polypeptide derived from or SEQ ID NO: 14 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 14. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 14. The polypeptide of any of the embodiments above related to SEQ ID NO: 14 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 14. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 13. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 13. In another embodiment, the polypeptide is derived from SEQ ID NO: 14 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 14 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 14 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 16; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 15; (c) a polypeptide derived from or SEQ ID NO: 16 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 16. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 16. The polypeptide of any of the embodiments above related to SEQ ID NO: 16 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 16. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 15. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 15. In another embodiment, the polypeptide is derived from SEQ ID NO: 16 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 16 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 16 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 18; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 17; (c) a polypeptide derived from or SEQ ID NO: 18 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 18. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 18. The polypeptide of any of the embodiments above related to SEQ ID NO: 18 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 18. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 17. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 17. In another embodiment, the polypeptide is derived from SEQ ID NO: 18 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 18 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions 26 introduced into the polypeptide of SEQ ID NO: 18 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 20; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 19; (c) a polypeptide derived from or SEQ ID NO: 20 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 20. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 20. The polypeptide of any of the embodiments above related to SEQ ID NO: 20 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 20. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 19. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 19. In another embodiment, the polypeptide is derived from SEQ ID NO: 20 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 20 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 20 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 22; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 21; (c) a polypeptide derived from or SEQ ID NO: 22 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 22. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 22. The polypeptide of any of the embodiments above related to SEQ ID NO: 22 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 22. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 21. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 21. In another embodiment, the polypeptide is derived from SEQ ID NO: 22 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 22 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 22 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 24; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 23; (c) a polypeptide derived from or SEQ ID NO: 24 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 24. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 24. The polypeptide of any of the embodiments above related to SEQ ID NO: 24 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 24. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 23. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 23. In another embodiment, the polypeptide is derived from SEQ ID NO: 24 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 24 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 24 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a) a polypeptide having at least 60% sequence identity to SEQ ID NO: 26; (b) a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 25; (c) a polypeptide derived from or SEQ ID NO: 26 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 26. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 26. The polypeptide of any of the embodiments above related to SEQ ID NO: 26 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 26. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 25. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 25. In another embodiment, the polypeptide is derived from SEQ ID NO: 26 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 26 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 26 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 28; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 27; (c) a polypeptide derived from or SEQ ID NO: 28 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 28. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 28. The polypeptide of any of the embodiments above related to SEQ ID NO: 28 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 28. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 27. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 27. In another embodiment, the polypeptide is derived from SEQ ID NO: 28 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 28 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 28 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 30; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 29; (c) a polypeptide derived from or SEQ ID NO: 30 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 30. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 30. The polypeptide of any of the embodiments above related to SEQ ID NO: 30 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 30. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 29. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 29. In another embodiment, the polypeptide is derived from SEQ ID NO: 30 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 30 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 30 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 32; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 31; (c) a polypeptide derived from or SEQ ID NO: 32 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 32. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 32. The polypeptide of any of the embodiments above related to SEQ ID NO: 32 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 32. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 31. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 31. In another embodiment, the polypeptide is derived from SEQ ID NO: 32 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 32 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 32 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 34; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 33; (c) a polypeptide derived from or SEQ ID NO: 34 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 34. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 34. The polypeptide of any of the embodiments above related to SEQ ID NO: 34 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 34. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 33. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 33. In another embodiment, the polypeptide is derived from SEQ ID NO: 34 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 34 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 34 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 36; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 35; (c) a polypeptide derived from or SEQ ID NO: 36 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 36. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 36. The polypeptide of any of the embodiments above related to SEQ ID NO: 36 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 36. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 35. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 35. In another embodiment, the polypeptide is derived from SEQ ID NO: 36 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 36 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 36 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 38; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 37; (c) a polypeptide derived from or SEQ ID NO: 38 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 38. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 38. The polypeptide of any of the embodiments above related to SEQ ID NO: 38 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 38. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 37. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 37. In another embodiment, the polypeptide is derived from SEQ ID NO: 38 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 38 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 38 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 40; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 39; (c) a polypeptide derived from or SEQ ID NO: 40 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 40. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 40. The polypeptide of any of the embodiments above related to SEQ ID NO: 40 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 40. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 39. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 39. In another embodiment, the polypeptide is derived from SEQ ID NO: 40 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 40 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 40 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 42; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 41; (c) a polypeptide derived from or SEQ ID NO: 42 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 42. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 42. The polypeptide of any of the embodiments above related to SEQ ID NO: 42 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 42. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 41. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 41. In another embodiment, the polypeptide is derived from SEQ ID NO: 42 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 42 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 42 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 44; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 43; (c) a polypeptide derived from or SEQ ID NO: 44 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 44. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 44. The polypeptide of any of the embodiments above related to SEQ ID NO: 44 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 44. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 43. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 43. In another embodiment, the polypeptide is derived from SEQ ID NO: 44 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 44 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 44 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 46; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 45; (c) a polypeptide derived from or SEQ ID NO: 46 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 46. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 46. The polypeptide of any of the embodiments above related to SEQ ID NO: 46 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 46. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 45. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 45. In another embodiment, the polypeptide is derived from SEQ ID NO: 46 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 46 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 46 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 48; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 47; (c) a polypeptide derived from or SEQ ID NO: 48 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 48. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 48. The polypeptide of any of the embodiments above related to SEQ ID NO: 48 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 48. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, 40 at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 47. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 47. In another embodiment, the polypeptide is derived from SEQ ID NO: 48 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 48 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 48 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 50; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 49; (c) a polypeptide derived from or SEQ ID NO: 50 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 50. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 50. The polypeptide of any of the embodiments above related to SEQ ID NO: 50 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 50. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 49. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 49. In another embodiment, the polypeptide is derived from SEQ ID NO: 50 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 50 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 50 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 52; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 51; (c) a polypeptide derived from or SEQ ID NO: 52 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 52. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 52. The polypeptide of any of the embodiments above related to SEQ ID NO: 52 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 52. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 51. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 51. In another embodiment, the polypeptide is derived from SEQ ID NO: 52 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 52 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 52 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 54; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 53; (c) a polypeptide derived from or SEQ ID NO: 54 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 54. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 54. The polypeptide of any of the embodiments above related to SEQ ID NO: 54 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 54. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 53. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 53. In another embodiment, the polypeptide is derived from SEQ ID NO: 54 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 54 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 54 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 56; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 55; (c) a polypeptide derived from or SEQ ID NO: 56 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 56. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 56. The polypeptide of any of the embodiments above related to SEQ ID NO: 56 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 56. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 55. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 55. In another embodiment, the polypeptide is derived from SEQ ID NO: 56 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 56 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 56 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 58; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 57; (c) a polypeptide derived from or SEQ ID NO: 58 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 58. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 58. The polypeptide of any of the embodiments above related to SEQ ID NO: 58 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 58. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 57. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 57. In another embodiment, the polypeptide is derived from SEQ ID NO: 58 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 58 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions 45 introduced into the polypeptide of SEQ ID NO: 58 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 60; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 59; (c) a polypeptide derived from or SEQ ID NO: 60 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 60. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 60. The polypeptide of any of the embodiments above related to SEQ ID NO: 60 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 60. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 59. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 59. In another embodiment, the polypeptide is derived from SEQ ID NO: 60 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 60 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 60 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 62; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 61; (c) a polypeptide derived from or SEQ ID NO: 62 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 62. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 62. The polypeptide of any of the embodiments above related to SEQ ID NO: 62 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 62. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 61. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 61. In another embodiment, the polypeptide is derived from SEQ ID NO: 62 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 62 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 62 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 64; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 63; (c) a polypeptide derived from or SEQ ID NO: 64 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 64. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 64. The polypeptide of any of the embodiments above related to SEQ ID NO: 64 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 64. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 63. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 63. In another embodiment, the polypeptide is derived from SEQ ID NO: 64 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 64 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 64 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a) a polypeptide having at least 60% sequence identity to SEQ ID NO: 66; (b) a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 65; (c) a polypeptide derived from or SEQ ID NO: 66 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 66. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 66. The polypeptide of any of the embodiments above related to SEQ ID NO: 66 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 66. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 65. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 65. In another embodiment, the polypeptide is derived from SEQ ID NO: 66 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 66 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 66 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 68; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 67; (c) a polypeptide derived from or SEQ ID NO: 68 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 68. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 68. The polypeptide of any of the embodiments above related to SEQ ID NO: 68 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 68. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 67. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 67. In another embodiment, the polypeptide is derived from SEQ ID NO: 68 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 68 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 68 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 70; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 69; (c) a polypeptide derived from or SEQ ID NO: 70 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 70. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 70. The polypeptide of any of the embodiments above related to SEQ ID NO: 70 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 70. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 69. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 69. In another embodiment, the polypeptide is derived from SEQ ID NO: 70 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 70 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 70 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 72; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 71; (c) a polypeptide derived from or SEQ ID NO: 72 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 72. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 72. The polypeptide of any of the embodiments above related to SEQ ID NO: 72 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 72. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 71. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 71. In another embodiment, the polypeptide is derived from SEQ ID NO: 72 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 72 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 72 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 74; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 73; (c) a polypeptide derived from or SEQ ID NO: 74 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 74. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 74. The polypeptide of any of the embodiments above related to SEQ ID NO: 74 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 74. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 73. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 73. In another embodiment, the polypeptide is derived from SEQ ID NO: 74 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 74 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 74 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 76; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 75; (c) a polypeptide derived from or SEQ ID NO: 76 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 76. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 76. The polypeptide of any of the embodiments above related to SEQ ID NO: 76 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 76. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 75. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 75. In another embodiment, the polypeptide is derived from SEQ ID NO: 76 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 76 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 76 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 79; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 78; (c) a polypeptide derived from or SEQ ID NO: 79 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 79. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 79. The polypeptide of any of the embodiments above related to SEQ ID NO: 79 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 79. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 78. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 78. In another embodiment, the polypeptide is derived from SEQ ID NO: 79 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 79 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 79 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 81; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 80; (c) a polypeptide derived from or SEQ ID NO: 81 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 81. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 81. The polypeptide of any of the embodiments above related to SEQ ID NO: 81 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 81. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 80. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 80. In another embodiment, the polypeptide is derived from SEQ ID NO: 81 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 81 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 81 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 83; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 82; (c) a polypeptide derived from or SEQ ID NO: 83 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 83. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 83. The polypeptide of any of the embodiments above related to SEQ ID NO: 83 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 83. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 82. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 82. In another embodiment, the polypeptide is derived from SEQ ID NO: 83 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 83 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 83 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. In another aspect, the invention relates to polypeptides having carbonic anhydrase activity, selected from the group consisting of: (a)    a polypeptide having at least 60% sequence identity to SEQ ID NO: 85; (b)    a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of SEQ ID NO: 84; (c) a polypeptide derived from or SEQ ID NO: 85 by substitution, deletion or addition of one or several amino acids; (d) a polypeptide derived from the polypeptide of (a), (b), or (c) wherein the N- and / or C-terminal end has been extended by the addition of one or more amino acids; and (e) a fragment of the polypeptide of (a), (b), or (c); wherein the polypeptide has carbonic anhydrase activity. In one embodiment, the polypeptide has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 85. In one embodiment, the polypeptide comprises, consists essentially of, or consists of the amino acid sequence of SEQ ID NO: 85. The polypeptide of any of the embodiments above related to SEQ ID NO: 85 may have an N-terminal and / or C-terminal extension of one or more amino acids, e.g., 1-5 amino acids. In another embodiment, the polypeptide is a fragment comprising at least 85%, 90%, or 95% of the number of amino acids of SEQ ID NO: 85. In some embodiments, the polypeptide is encoded by a polynucleotide having a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to the coding sequence of SEQ ID NO: 84. The polynucleotide encoding the polypeptide preferably comprises, consists essentially of, or consists of SEQ ID NO: 84. In another embodiment, the polypeptide is derived from SEQ ID NO: 85 by substitution, deletion or addition of one or more amino acids. In some embodiments, the polypeptide is a variant of SEQ ID NO: 85 comprising a substitution, deletion, and / or insertion at one or more positions. In one embodiment, the number of amino acid substitutions, deletions and / or insertions introduced into the polypeptide of SEQ ID NO: 85 is up to 15, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15. The amino acid changes may be of a minor nature, that is conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1-30 amino acids; small amino- or carboxyl-terminal extensions, such as an amino-terminal methionine residue; a small linker peptide of up to 20-25 residues; or a small extension that facilitates purification by changing net charge or another function, such as a poly-histidine tract, an antigenic epitope or a binding module. Examples of conservative substitutions are within the groups of basic amino acids (arginine, lysine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine and valine), aromatic amino acids (phenylalanine, tryptophan and tyrosine), and small amino acids (glycine, alanine, serine, threonine and methionine). Amino acid substitutions that do not generally alter specific activity are known in the art and are described, for example, by H. Neurath and R.L. Hill, 1979, In, The Proteins, Academic Press, New York. Common substitutions are Ala / Ser, Val / lle, Asp / Glu, Thr / Ser, Ala / Gly, Ala / Thr, Ser / Asn, Ala / Val, Ser / Gly, Tyr / Phe, Ala / Pro, Lys / Arg, Asp / Asn, Leu / lle, Leu / Val, Ala / Glu, and Asp / Gly. Alternatively, the amino acid changes are of such a nature that the physico-chemical properties of the polypeptides are altered. For example, amino acid changes may improve the thermal stability of the polypeptide, alter the substrate specificity, change the pH optimum, and the like. Essential amino acids in a polypeptide can be identified according to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham and Wells, 1989, Science 244: 1081-1085). In the latter technique, single alanine mutations are 58 introduced at every residue in the molecule, and the resultant molecules are tested for carbonic anhydrase activity to identify amino acid residues that are critical to the activity of the molecule. See also, Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708. The active site of the enzyme or other biological interaction can also be determined by physical analysis of structure, as determined by such techniques as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, in conjunction with mutation of putative contact site amino acids. See, for example, de Vos et al., 1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224: 899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64. The identity of essential amino acids can also be inferred from an alignment with a related polypeptide, and / or be inferred from sequence homology and conserved catalytic machinery with a related polypeptide or within a polypeptide or protein family with polypeptides / proteins descending from a common ancestor, typically having similar three-dimensional structures, functions, and significant sequence similarity. Additionally or alternatively, protein structure prediction tools can be used for protein structure modelling to identify essential amino acids and / or active sites of polypeptides. See, for example, Jumper et al., 2021, “Highly accurate protein structure prediction with AlphaFold”, Nature 596: 583-589. Alpha-carbonic anhydrases may be identified by the consensus sequence motif: S-E-[HN]-x-[LIVM]-x(4)-[FYH]-x(2)-E-[LIVMGA]-H-[LIVMFA](2). In one embodiment, the carbonic anhydrase comprises the consensus sequence motif S-E-[HN]-x-[LIVM]-x(4)-[FYH]-x(2)-E-[LIVMGA]-H-[LIVMFA](2). Additional guidance on the structure-activity relationship of the carbonic anhydrases herein can be determined using multiple sequence alignment (MSA) techniques well-known in the art. Based on the teachings herein, the skilled artisan could make similar alignments with any number of carbonic anhydrases described herein or known in the art. Such alignments aid the skilled artisan to determine potentially relevant domains (e.g., binding domains or catalytic domains), as well as which amino acid residues are conserved and not conserved among the different carbonic anhydrase sequences. It is appreciated in the art that changing an amino acid that is conserved at a particular position between disclosed polypeptides will more likely result in a change in biological activity (Bowie et al., 1990, Science 247: 1306-1310: “Residues that are directly involved in protein functions such as binding or catalysis will certainly be among the most conserved”). In contrast, substituting an amino acid that is not highly conserved among the polypeptides will not likely or significantly alter the biological activity. Even further guidance on the structure-activity relationship for the skilled artisan can be found in published x-ray crystallography studies known in the art. A crystal structure of the Persephonella marina a-carbonic anhydrase identified active site residues, the calcium binding site, and disulfide residues important for thermostability (Kim etal., 2019, Mol. Cells. 42(6): 460469). Amino acid residues H107, H109, and H126 are predicted to form a histidine triad which is important for catalysis (corresponding to positions H86, H88, and H105 for the P. marina mature 59 polypeptide sequence of SEQ ID NO: 77). Amino acid residues C44 and C197 are predicted to form a disulfide bridge to provide conformational and thermal stability by increasing structural rigidity (corresponding to positions C23 and C176 for the P. marina mature polypeptide sequence of SEQ ID NO: 77). Amino acid residues Y25, H82, E113 and T193 are predicted to participate in a proton shuttle mechanism, which also is relevant for the catalytic activity of the enzyme (corresponding to positions Y4, H61, E92 and T172 for the P. marina mature polypeptide sequence of SEQ ID NO: 77). Amino acid residues V128, V138, L136, L192, V201 and W203 are predicted to be responsible for CO2 binding (corresponding to positions V107, V117, L115, L171, V180 and W182 for the P. marina mature polypeptide sequence of SEQ ID NO: 77). The Endozoicomonas arenosclerae carbonic anhydrase of SEQ ID NO: 2 contains key amino acid residues that may be important for activity (See alignment in Figure 8). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 89, 91, and / or 108 of SEQ ID NO: 2. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 26 and / or 179 of SEQ ID NO: 2. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 7 of SEQ ID NO: 2, a histidine at a position corresponding to position 64 of SEQ ID NO: 2, a glutamic acid at a position correspondning to position 95 of SEQ ID NO: 2 and / or a threonine at a position correspondning to position 175 of SEQ ID NO: 2. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 110 of SEQ ID NO: 2, a leucine at a position correspondning to position 118 of SEQ ID NO: 2, a valine at a position corresponding to position 120 of SEQ ID NO: 2, a leucine at a position correspondning to position 174 of SEQ ID NO: 2, a valine at a position correspondning to position 183 of SEQ ID NO: 2 and / or a tryptophan at a position correspondning to position 185 of SEQ ID NO: 2. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The Achromatium sp. carbonic anhydrase of SEQ ID NO: 4 contains key amino acid residues that may be important for activity (See alignment in Figure 9). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 92, 94, and / or 111 of SEQ ID NO: 4. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 28 and / or 184 of SEQ ID NO: 4. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 9 of SEQ ID NO: 4, a histidine at a position corresponding to position 67 of SEQ ID NO: 4, a glutamic acid at a position correspondning to position 98 of SEQ ID NO: 4 and / or a threonine at a position correspondning to position 180 of 60 SEQ ID NO: 4. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 113 of SEQ ID NO: 4, a leucine at a position correspondning to position 121 of SEQ ID NO: 4, a valine at a position corresponding to position 123 of SEQ ID NO: 4, a leucine at a position correspondning to position 171 of SEQ ID NO: 4, a valine at a position correspondning to position 188 of SEQ ID NO: 4 and / or a tryptophan at a position correspondning to position 190 of SEQ ID NO: 4. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The Endozoicomonas numazuensis carbonic anhydrase of SEQ ID NO: 6 contains key amino acid residues that may be important for activity (See alignment in Figure 10). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 89, 91, and / or 108 of SEQ ID NO: 6. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 26 and / or 179 of SEQ ID NO: 6. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 7 of SEQ ID NO: 6, a histidine at a position corresponding to position 64 of SEQ ID NO: 6, a glutamic acid at a position correspondning to position 95 of SEQ ID NO: 6 and / or a threonine at a position correspondning to position 175 of SEQ ID NO: 6. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 110 of SEQ ID NO: 6, a leucine at a position correspondning to position 118 of SEQ ID NO: 6, a valine at a position corresponding to position 120 of SEQ ID NO: 6, a leucine at a position correspondning to position 174 of SEQ ID NO: 6, a valine at a position correspondning to position 183 of SEQ ID NO: 6 and / or a tryptophan at a position correspondning to position 185 of SEQ ID NO: 6. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The Thiorhodococcus drewsii carbonic anhydrase of SEQ ID NO: 8 contains key amino acid residues that may be important for activity (See alignment in Figure 11). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 88, 90, and / or 107 of SEQ ID NO: 8. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 25 and / or 178 of SEQ ID NO: 8. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 6 of SEQ ID NO: 8, a histidine at a position 61 corresponding to position 63 of SEQ ID NO: 8, a glutamic acid at a position correspondning to position 94 of SEQ ID NO: 8 and / or a threonine at a position correspondning to position 174 of SEQ ID NO: 8. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 109 of SEQ ID NO: 8, a leucine at a position correspondning to position 117 of SEQ ID NO: 8, a valine at a position corresponding to position 119 of SEQ ID NO: 8, a leucine at a position correspondning to position 173 of SEQ ID NO: 8, a valine at a position correspondning to position 182 of SEQ ID NO: 8 and / or a tryptophan at a position correspondning to position 184 of SEQ ID NO: 8. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 10 contains key amino acid residues that may be important for activity (See alignment in Figure 12). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 95, 97, and / or 114 of SEQ ID NO: 10. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 32 and / or 186 of SEQ ID NO: 10. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 4 of SEQ ID NO: 10, a histidine at a position corresponding to position 70 of SEQ ID NO: 10, a glutamic acid ata position correspondning to position 101 of SEQ ID NO: 10 and / or a threonine at a position correspondning to position 182 of SEQ ID NO: 10. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 116 of SEQ ID NO: 10, a leucine ata position correspondning to position 124 of SEQ ID NO: 10, a valine at a position corresponding to position 126 of SEQ ID NO: 10, a leucine at a position correspondning to position 181 of SEQ ID NO: 10, a valine at a position correspondning to position 190 of SEQ ID NO: 10 and / or a tryptophan at a position correspondning to position 192 of SEQ ID NO: 10. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 12 contains key amino acid residues that may be important for activity (See alignment in Figure 13). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 90, 92, and / or 109 of SEQ ID NO: 12. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 27 and / or 180 of SEQ ID NO: 12. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 62 corresponding to position 8 of SEQ ID NO: 12, a histidine at a position corresponding to position 65 of SEQ ID NO: 12, a glutamic acid at a position correspondning to position 962 of SEQ ID NO: 12 and / or a threonine at a position correspondning to position 176 of SEQ ID NO: 12. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 111 of SEQ ID NO: 12, a leucine at a position correspondning to position 119 of SEQ ID NO: 12, a valine at a position corresponding to position 121 of SEQ ID NO: 12, a leucine at a position correspondning to position 175 of SEQ ID NO: 12, a valine at a position correspondning to position 184 of SEQ ID NO: 12 and / or a tryptophan at a position correspondning to position 186 of SEQ ID NO: 12. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The Aquificales bacterium carbonic anhydrase of SEQ ID NO: 14 contains key amino acid residues that may be important for activity (See alignment in Figure 14). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 97, 99, and / or 116 of SEQ ID NO: 14. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 32 and / or 187 of SEQ ID NO: 14. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 13 of SEQ ID NO: 14, a histidine at a position corresponding to position 72 of SEQ ID NO: 14, a glutamic acid at a position correspondning to position 103 of SEQ ID NO: 14 and / or a threonine ata position correspondning to position 183 of SEQ ID NO: 14. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 118 of SEQ ID NO: 14, a valine at a position corresponding to position 128 of SEQ ID NO: 14, a leucine at a position correspondning to position 182 of SEQ ID NO: 14, a valine at a position correspondning to position 191 of SEQ ID NO: 14 and / or a tryptophan at a position correspondning to position 193 of SEQ ID NO: 14. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, or at least five residues. The carbonic anhydrase of SEQ ID NO: 16 contains key amino acid residues that may be important for activity (See alignment in Figure 15). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 87, 89, and / or 106 of SEQ ID NO: 16. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 16 and / or 177 of SEQ ID NO: 16. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 63 corresponding to position 5 of SEQ ID NO: 16, a histidine at a position corresponding to position 62 of SEQ ID NO: 16, a glutamic acid at a position correspondning to position 93 of SEQ ID NO: 16 and / or a threonine at a position correspondning to position 173 of SEQ ID NO: 16. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 108 of SEQ ID NO: 16, a leucine ata position correspondning to position 116 of SEQ ID NO: 16, a valine at a position corresponding to position 118 of SEQ ID NO: 16, a leucine at a position correspondning to position 172 of SEQ ID NO: 16, a valine at a position correspondning to position 181 of SEQ ID NO: 16 and / or a tryptophan at a position correspondning to position 183 of SEQ ID NO: 16. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 18 contains key amino acid residues that may be important for activity (See alignment in Figure 16). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 90, 92, and / or 109 of SEQ ID NO: 18. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 27 and / or 181 of SEQ ID NO: 18. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 8 of SEQ ID NO: 18, a histidine at a position corresponding to position 65 of SEQ ID NO: 18, a glutamic acid at a position correspondning to position 96 of SEQ ID NO: 18 and / or a threonine at a position correspondning to position 177 of SEQ ID NO: 18. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 111 of SEQ ID NO: 18, a leucine at a position correspondning to position 119 of SEQ ID NO: 18, a valine at a position corresponding to position 121 of SEQ ID NO: 18, a leucine at a position correspondning to position 185 of SEQ ID NO: 18, a valine at a position correspondning to position 180 of SEQ ID NO: 18 and / or a tryptophan at a position correspondning to position 187 of SEQ ID NO: 18. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 20 contains key amino acid residues that may be important for activity (See alignment in Figure 17). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 87, 89, and / or 106 of SEQ ID NO: 20. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 24 and / or 176 of SEQ ID NO: 20. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 64 corresponding to position 5 of SEQ ID NO: 20, a histidine at a position corresponding to position 62 of SEQ ID NO: 20, a glutamic acid at a position correspondning to position 93 of SEQ ID NO: 20 and / or a threonine at a position correspondning to position 172 of SEQ ID NO: 20. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 108 of SEQ ID NO: 20, a leucine ata position correspondning to position 116 of SEQ ID NO: 20, a valine at a position corresponding to position 118 of SEQ ID NO: 20, a leucine at a position correspondning to position 171 of SEQ ID NO: 20, a valine at a position correspondning to position 180 of SEQ ID NO: 20 and / or a tryptophan at a position correspondning to position 182 of SEQ ID NO: 20. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 22 contains key amino acid residues that may be important for activity (See alignment in Figure 18). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 98, 100, and / or 117 of SEQ ID NO: 22. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 35 and / or 188 of SEQ ID NO: 22. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 16 of SEQ ID NO: 22, a histidine at a position corresponding to position 73 of SEQ ID NO: 22, a glutamic acid at a position correspondning to position 104 of SEQ ID NO: 22 and / or a threonine at a position correspondning to position 184 of SEQ ID NO: 22. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 119 of SEQ ID NO: 22, a leucine ata position correspondning to position 127 of SEQ ID NO: 22, a valine at a position corresponding to position 129 of SEQ ID NO: 22, a leucine at a position correspondning to position 183 of SEQ ID NO: 22, a valine at a position correspondning to position 192 of SEQ ID NO: 22 and / or a tryptophan at a position correspondning to position 194 of SEQ ID NO: 22. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 26 contains key amino acid residues that may be important for activity (See alignment in Figure 19). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 87, 89, and / or 106 of SEQ ID NO: 26. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 24 and / or 177 of SEQ ID NO: 26. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 65 corresponding to position 5 of SEQ ID NO: 26, a histidine at a position corresponding to position 62 of SEQ ID NO: 26, a glutamic acid at a position correspondning to position 93 of SEQ ID NO: 26 and / or a threonine at a position correspondning to position 173 of SEQ ID NO: 26. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 108 of SEQ ID NO: 26, a leucine ata position correspondning to position 116 of SEQ ID NO: 26, a valine at a position corresponding to position 118 of SEQ ID NO: 26, a leucine at a position correspondning to position 172 of SEQ ID NO: 26, a valine at a position correspondning to position 181 of SEQ ID NO: 26 and / or a tryptophan at a position correspondning to position 183 of SEQ ID NO: 26. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 28 contains key amino acid residues that may be important for activity (See alignment in Figure 20). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 87, 89, and / or 106 of SEQ ID NO: 28. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 24 and / or 177 of SEQ ID NO: 28. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 5 of SEQ ID NO: 28, a histidine at a position corresponding to position 62 of SEQ ID NO: 28, a glutamic acid at a position correspondning to position 93 of SEQ ID NO: 28 and / or a threonine at a position correspondning to position 173 of SEQ ID NO: 28. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 108 of SEQ ID NO: 28, a leucine ata position correspondning to position 116 of SEQ ID NO: 28, a valine at a position corresponding to position 118 of SEQ ID NO: 28, a leucine at a position correspondning to position 172 of SEQ ID NO: 28, a valine at a position correspondning to position 181 of SEQ ID NO: 28 and / or a tryptophan at a position correspondning to position 183 of SEQ ID NO: 28. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 30 contains key amino acid residues that may be important for activity (See alignment in Figure 21). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 86, 88, and / or 105 of SEQ ID NO: 30. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 24 and / or 175 of SEQ ID NO: 30. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 66 corresponding to position 5 of SEQ ID NO: 30, a histidine at a position corresponding to position 61 of SEQ ID NO: 30, a glutamic acid at a position correspondning to position 92 of SEQ ID NO: 30 and / or a threonine at a position correspondning to position 171 of SEQ ID NO: 30. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 107 of SEQ ID NO: 30, a leucine ata position correspondning to position 115 of SEQ ID NO: 30, a valine at a position corresponding to position 117 of SEQ ID NO: 30, a leucine at a position correspondning to position 171 of SEQ ID NO: 30, a valine at a position correspondning to position 179 of SEQ ID NO: 30 and / or a tryptophan at a position correspondning to position 181 of SEQ ID NO: 30. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 32 contains key amino acid residues that may be important for activity (See alignment in Figure 22). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 87, 89, and / or 106 of SEQ ID NO: 32. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 24 and / or 177 of SEQ ID NO: 32. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 5 of SEQ ID NO: 32, a histidine at a position corresponding to position 62 of SEQ ID NO: 32, a glutamic acid at a position correspondning to position 93 of SEQ ID NO: 32 and / or a threonine at a position correspondning to position 173 of SEQ ID NO: 32. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 108 of SEQ ID NO: 32, a leucine ata position correspondning to position 116 of SEQ ID NO: 32, a valine at a position corresponding to position 118 of SEQ ID NO: 32, a leucine at a position correspondning to position 172 of SEQ ID NO: 32, a valine at a position correspondning to position 181 of SEQ ID NO: 32 and / or a tryptophan at a position correspondning to position 183 of SEQ ID NO: 32. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 34 contains key amino acid residues that may be important for activity (See alignment in Figure 23). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 87, 89, and / or 106 of SEQ ID NO: 34. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 25 and / or 177 of SEQ ID NO: 34. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 67 corresponding to position 6 of SEQ ID NO: 34, a histidine at a position corresponding to position 62 of SEQ ID NO: 34, a glutamic acid at a position correspondning to position 93 of SEQ ID NO: 34 and / or a threonine at a position correspondning to position 173 of SEQ ID NO: 34. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 108 of SEQ ID NO: 34, a leucine ata position correspondning to position 116 of SEQ ID NO: 34, a valine at a position corresponding to position 118 of SEQ ID NO: 34, a leucine at a position correspondning to position 172 of SEQ ID NO: 34, a valine at a position correspondning to position 181 of SEQ ID NO: 34 and / or a tryptophan at a position correspondning to position 183 of SEQ ID NO: 34. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 36 contains key amino acid residues that may be important for activity (See alignment in Figure 24). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 91, 93, and / or 110 of SEQ ID NO: 36. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 25 and / or 182 of SEQ ID NO: 36. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 6 of SEQ ID NO: 36, a histidine at a position corresponding to position 66 of SEQ ID NO: 36, a glutamic acid at a position correspondning to position 97 of SEQ ID NO: 36 and / or a threonine at a position correspondning to position 178 of SEQ ID NO: 36. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 112 of SEQ ID NO: 36, a leucine at a position correspondning to position 120 of SEQ ID NO: 36, a valine at a position corresponding to position 122 of SEQ ID NO: 36, a leucine at a position correspondning to position 177 of SEQ ID NO: 36, a valine at a position correspondning to position 186 of SEQ ID NO: 36 and / or a tryptophan at a position correspondning to position 188 of SEQ ID NO: 36. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 38 contains key amino acid residues that may be important for activity (See alignment in Figure 25). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 89, 91, and / or 108 of SEQ ID NO: 38. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 26 and / or 179 of SEQ ID NO: 38. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 68 corresponding to position 7 of SEQ ID NO: 38, a histidine at a position corresponding to position 64 of SEQ ID NO: 38, a glutamic acid at a position correspondning to position 95 of SEQ ID NO: 38 and / or a threonine at a position correspondning to position 175 of SEQ ID NO: 38. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 110 of SEQ ID NO: 38, a leucine at a position correspondning to position 118 of SEQ ID NO: 38, a valine at a position corresponding to position 120 of SEQ ID NO: 38, a leucine at a position correspondning to position 174 of SEQ ID NO: 38, a valine at a position correspondning to position 183 of SEQ ID NO: 38 and / or a tryptophan at a position correspondning to position 185 of SEQ ID NO: 38. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 40 contains key amino acid residues that may be important for activity (See alignment in Figure 26). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 89, 91, and / or 108 of SEQ ID NO: 40. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 27 and / or 179 of SEQ ID NO: 40. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 8 of SEQ ID NO: 40, a histidine at a position corresponding to position 64 of SEQ ID NO: 40, a glutamic acid at a position correspondning to position 95 of SEQ ID NO: 40 and / or a threonine at a position correspondning to position 175 of SEQ ID NO: 40. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 110 of SEQ ID NO: 40, a leucine at a position correspondning to position 118 of SEQ ID NO: 40, a valine at a position corresponding to position 120 of SEQ ID NO: 40, a leucine at a position correspondning to position 174 of SEQ ID NO: 40, a valine at a position correspondning to position 183 of SEQ ID NO: 40 and / or a tryptophan at a position correspondning to position 185 of SEQ ID NO: 40. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 42 contains key amino acid residues that may be important for activity (See alignment in Figure 27). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 87, 89, and / or 106 of SEQ ID NO: 42. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 25 and / or 176 of SEQ ID NO: 42. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 69 corresponding to position 6 of SEQ ID NO: 42, a histidine at a position corresponding to position 42 of SEQ ID NO: 42, a glutamic acid at a position correspondning to position 93 of SEQ ID NO: 42 and / or a threonine at a position correspondning to position 172 of SEQ ID NO: 42. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 108 of SEQ ID NO: 42, a leucine ata position correspondning to position 116 of SEQ ID NO: 42, a valine at a position corresponding to position 118 of SEQ ID NO: 42, a leucine at a position correspondning to position 171 of SEQ ID NO: 42, a valine at a position correspondning to position 180 of SEQ ID NO: 42 and / or a tryptophan at a position correspondning to position 182 of SEQ ID NO: 42. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 44 contains key amino acid residues that may be important for activity (See alignment in Figure 28). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 87, 89, and / or 106 of SEQ ID NO: 44. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 24 and / or 177 of SEQ ID NO: 44. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 5 of SEQ ID NO: 44, a histidine at a position corresponding to position 62 of SEQ ID NO: 44, a glutamic acid at a position correspondning to position 93 of SEQ ID NO: 44 and / or a threonine at a position correspondning to position 173 of SEQ ID NO: 44. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 108 of SEQ ID NO: 44, a leucine ata position correspondning to position 116 of SEQ ID NO: 44, a valine at a position corresponding to position 118 of SEQ ID NO: 44, a leucine at a position correspondning to position 172 of SEQ ID NO: 44, a valine at a position correspondning to position 181 of SEQ ID NO: 44 and / or a tryptophan at a position correspondning to position 183 of SEQ ID NO: 44. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 46 contains key amino acid residues that may be important for activity (See alignment in Figure 29). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 90, 92, and / or 109 of SEQ ID NO: 46. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 27 and / or 180 of SEQ ID NO: 46. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 70 corresponding to position 8 of SEQ ID NO: 46, a histidine at a position corresponding to position 65 of SEQ ID NO: 46, a glutamic acid at a position correspondning to position 96 of SEQ ID NO: 46 and / or a threonine at a position correspondning to position 176 of SEQ ID NO: 46. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 111 of SEQ ID NO: 46, a leucine at a position correspondning to position 119 of SEQ ID NO: 46, a valine at a position corresponding to position 121 of SEQ ID NO: 46, a leucine at a position correspondning to position 175 of SEQ ID NO: 46, a valine at a position correspondning to position 184 of SEQ ID NO: 46 and / or a tryptophan at a position correspondning to position 186 of SEQ ID NO: 46. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 48 contains key amino acid residues that may be important for activity (See alignment in Figure 30). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 89, 91, and / or 108 of SEQ ID NO: 48. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 26 and / or 180 of SEQ ID NO: 48. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 6 of SEQ ID NO: 48, a histidine at a position corresponding to position 64 of SEQ ID NO: 48, a glutamic acid at a position correspondning to position 95 of SEQ ID NO: 48 and / or a threonine at a position correspondning to position 176 of SEQ ID NO: 48. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 109 of SEQ ID NO: 48, a leucine ata position correspondning to position 117 of SEQ ID NO: 48, a valine at a position corresponding to position 119 of SEQ ID NO: 48, a leucine at a position correspondning to position 175 of SEQ ID NO: 48, a valine at a position correspondning to position 184 of SEQ ID NO: 48 and / or a tryptophan at a position correspondning to position 186 of SEQ ID NO: 48. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 50 contains key amino acid residues that may be important for activity (See alignment in Figure 31). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 89, 91, and / or 108 of SEQ ID NO: 50. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 26 and / or 179 of SEQ ID NO: 50. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 71 corresponding to position 7 of SEQ ID NO: 50, a histidine at a position corresponding to position 64 of SEQ ID NO: 50, a glutamic acid at a position correspondning to position 95 of SEQ ID NO: 50 and / or a threonine at a position correspondning to position 175 of SEQ ID NO: 50. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 110 of SEQ ID NO: 50, a leucine at a position correspondning to position 118 of SEQ ID NO: 50, a valine at a position corresponding to position 120 of SEQ ID NO: 50, a leucine at a position correspondning to position 174 of SEQ ID NO: 50, a valine at a position correspondning to position 183 of SEQ ID NO: 50 and / or a tryptophan at a position correspondning to position 185 of SEQ ID NO: 50. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 52 contains key amino acid residues that may be important for activity (See alignment in Figure 32). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 86, 88, and / or 105 of SEQ ID NO: 52. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 23 and / or 176 of SEQ ID NO: 52. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 4 of SEQ ID NO: 52, a histidine at a position corresponding to position 61 of SEQ ID NO: 52, a glutamic acid at a position correspondning to position 92 of SEQ ID NO: 52 and / or a threonine at a position correspondning to position 172 of SEQ ID NO: 52. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 107 of SEQ ID NO: 52, a leucine ata position correspondning to position 115 of SEQ ID NO: 52, a valine at a position corresponding to position 117 of SEQ ID NO: 52, a leucine at a position correspondning to position 171 of SEQ ID NO: 52, a valine at a position correspondning to position 180 of SEQ ID NO: 52 and / or a tryptophan at a position correspondning to position 182 of SEQ ID NO: 52. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 54 contains key amino acid residues that may be important for activity (See alignment in Figure 33). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 85, 87, and / or 104 of SEQ ID NO: 54. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 22 and / or 175 of SEQ ID NO: 54. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 72 corresponding to position 3 of SEQ ID NO: 54, a histidine at a position corresponding to position 60 of SEQ ID NO: 54, a glutamic acid at a position correspondning to position 91 of SEQ ID NO: 54 and / or a threonine at a position correspondning to position 171 of SEQ ID NO: 54. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 106 of SEQ ID NO: 54, a leucine ata position correspondning to position 114 of SEQ ID NO: 54, a valine at a position corresponding to position 116 of SEQ ID NO: 54, a leucine at a position correspondning to position 170 of SEQ ID NO: 54, a valine at a position correspondning to position 179 of SEQ ID NO: 54 and / or a tryptophan at a position correspondning to position 181 of SEQ ID NO: 54. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 56 contains key amino acid residues that may be important for activity (See alignment in Figure 34). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 90, 92, and / or 109 of SEQ ID NO: 56. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 28 and / or 180 of SEQ ID NO: 56. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 9 of SEQ ID NO: 56, a histidine at a position corresponding to position 65 of SEQ ID NO: 56, a glutamic acid at a position correspondning to position 96 of SEQ ID NO: 56 and / or a threonine at a position correspondning to position 176 of SEQ ID NO: 56. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 111 of SEQ ID NO: 56, a leucine at a position correspondning to position 119 of SEQ ID NO: 56, a valine at a position corresponding to position 121 of SEQ ID NO: 56, a leucine at a position correspondning to position 175 of SEQ ID NO: 56, a valine at a position correspondning to position 184 of SEQ ID NO: 56 and / or a tryptophan at a position correspondning to position 186 of SEQ ID NO: 56. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 58 contains key amino acid residues that may be important for activity (See alignment in Figure 35). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 92, 94, and / or 111 of SEQ ID NO: 58. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 28 and / or 182 of SEQ ID NO: 58. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 73 corresponding to position 9 of SEQ ID NO: 58, a histidine at a position corresponding to position 66 of SEQ ID NO: 58, a glutamic acid at a position correspondning to position 98 of SEQ ID NO: 58 and / or a threonine at a position correspondning to position 178 of SEQ ID NO: 58. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 113 of SEQ ID NO: 58, a leucine at a position correspondning to position 121 of SEQ ID NO: 58, a valine at a position corresponding to position 123 of SEQ ID NO: 58, a leucine at a position correspondning to position 177 of SEQ ID NO: 58, a valine at a position correspondning to position 186 of SEQ ID NO: 58 and / or a tryptophan at a position correspondning to position 188 of SEQ ID NO: 58. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 60 contains key amino acid residues that may be important for activity (See alignment in Figure 36). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 85, 87, and / or 104 of SEQ ID NO: 60. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 20 and / or 175 of SEQ ID NO: 60. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 1 of SEQ ID NO: 60, a histidine at a position corresponding to position 58 of SEQ ID NO: 60, a glutamic acid at a position correspondning to position 91 of SEQ ID NO: 60 and / or a threonine at a position correspondning to position 171 of SEQ ID NO: 60. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 106 of SEQ ID NO: 60, a valine ata position corresponding to position 116 of SEQ ID NO: 60, a leucine at a position correspondning to position 170 of SEQ ID NO: 60, a valine at a position correspondning to position 179 of SEQ ID NO: 60 and / or a tryptophan at a position correspondning to position 181 of SEQ ID NO: 60. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, or at least five residues. The carbonic anhydrase of SEQ ID NO: 62 contains key amino acid residues that may be important for activity (See alignment in Figure 37). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 89, 91, and / or 108 of SEQ ID NO: 62. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 27 and / or 179 of SEQ ID NO: 62. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 74 corresponding to position 8 of SEQ ID NO: 62, a histidine at a position corresponding to position 64 of SEQ ID NO: 62, a glutamic acid at a position correspondning to position 95 of SEQ ID NO: 62 and / or a threonine at a position correspondning to position 175 of SEQ ID NO: 62. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 110 of SEQ ID NO: 62, a leucine at a position correspondning to position 118 of SEQ ID NO: 62, a valine at a position corresponding to position 120 of SEQ ID NO: 62, a leucine at a position correspondning to position 174 of SEQ ID NO: 62, a valine at a position correspondning to position 183 of SEQ ID NO: 62 and / or a tryptophan at a position correspondning to position 185 of SEQ ID NO: 62. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 64 contains key amino acid residues that may be important for activity (See alignment in Figure 38). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 91, 93, and / or 110 of SEQ ID NO: 64. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 25 and / or 112 of SEQ ID NO: 64. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 6 of SEQ ID NO: 64, a histidine at a position corresponding to position 63 of SEQ ID NO: 64, a glutamic acid at a position correspondning to position 97 of SEQ ID NO: 64 and / or a threonine at a position correspondning to position 177 of SEQ ID NO: 64. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 112 of SEQ ID NO: 64, a leucine at a position correspondning to position 120 of SEQ ID NO: 64, a valine at a position corresponding to position 122 of SEQ ID NO: 64, a leucine at a position correspondning to position 176 of SEQ ID NO: 64, a valine at a position correspondning to position 185 of SEQ ID NO: 64 and / or a tryptophan at a position correspondning to position 187 of SEQ ID NO: 64. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 66 contains key amino acid residues that may be important for activity (See alignment in Figure 39). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 88, 90, and / or 107 of SEQ ID NO: 66. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 25 and / or 178 of SEQ ID NO: 66. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 75 corresponding to position 6 of SEQ ID NO: 66, a histidine at a position corresponding to position 63 of SEQ ID NO: 66, a glutamic acid at a position correspondning to position 94 of SEQ ID NO: 66 and / or a threonine at a position correspondning to position 174 of SEQ ID NO: 66. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 109 of SEQ ID NO: 66, a leucine ata position correspondning to position 117 of SEQ ID NO: 66, a valine at a position corresponding to position 119 of SEQ ID NO: 66, a leucine at a position correspondning to position 173 of SEQ ID NO: 66, a valine at a position correspondning to position 182 of SEQ ID NO: 66 and / or a tryptophan at a position correspondning to position 184 of SEQ ID NO: 66. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 68 contains key amino acid residues that may be important for activity (See alignment in Figure 40). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 89, 91, and / or 108 of SEQ ID NO: 68. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 24 and / or 178 of SEQ ID NO: 68. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 5 of SEQ ID NO: 68, a histidine at a position corresponding to position 64 of SEQ ID NO: 68, a glutamic acid at a position correspondning to position 95 of SEQ ID NO: 68 and / or a threonine at a position correspondning to position 174 of SEQ ID NO: 68. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 110 of SEQ ID NO: 68, a leucine at a position correspondning to position 118 of SEQ ID NO: 68, a valine at a position corresponding to position 120 of SEQ ID NO: 68, a leucine at a position correspondning to position 173 of SEQ ID NO: 68, a valine at a position correspondning to position 182 of SEQ ID NO: 68 and / or a tryptophan at a position correspondning to position 184 of SEQ ID NO: 68. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 70 contains key amino acid residues that may be important for activity (See alignment in Figure 41). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 89, 91, and / or 108 of SEQ ID NO: 70. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 24 and / or 179 of SEQ ID NO: 70. In another embodiment, the carbonic anhydrase contains a tyrosine at a position 76 corresponding to position 4 of SEQ ID NO: 70, a histidine at a position corresponding to position 62 of SEQ ID NO: 70, a glutamic acid at a position correspondning to position 95 of SEQ ID NO: 70 and / or a threonine at a position correspondning to position 175 of SEQ ID NO: 70. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 110 of SEQ ID NO: 70, a leucine at a position correspondning to position 118 of SEQ ID NO: 70, a valine at a position corresponding to position 120 of SEQ ID NO: 70, a leucine at a position correspondning to position 174 of SEQ ID NO: 70, a valine at a position correspondning to position 183 of SEQ ID NO: 70 and / or a tryptophan at a position correspondning to position 185 of SEQ ID NO: 70. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The Trichophaea saccata carbonic anhydrase of SEQ ID NO: 74 contains key amino acid residues that may be important for activity (See alignment in Figure 42). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 102, 104, and / or 121 of SEQ ID NO: 74. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 34 and / or 195 of SEQ ID NO: 74. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 14 of SEQ ID NO: 74, a histidine at a position corresponding to position 72 of SEQ ID NO: 74, a glutamic acid at a position correspondning to position 108 of SEQ ID NO: 74 and / or a threonine ata position correspondning to position 191 of SEQ ID NO: 74. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 123 of SEQ ID NO: 74, a leucine at a position correspondning to position 131 of SEQ ID NO: 74, a valine at a position corresponding to position 133 of SEQ ID NO: 74, a leucine at a position correspondning to position 190 of SEQ ID NO: 74, a valine at a position correspondning to position 199 of SEQ ID NO: 74 and / or a tryptophan at a position correspondning to position 201 of SEQ ID NO: 74. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The Eleutherascus tuberculatus carbonic anhydrase of SEQ ID NO: 76 contains key amino acid residues that may be important for activity (See alignment in Figure 43). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 106, 108, and / or 125 of SEQ ID NO: 76. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to 77 position 34 and / or 202 of SEQ ID NO: 76. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 15 of SEQ ID NO: 76, a histidine at a position corresponding to position 72 of SEQ ID NO: 76, a glutamic acid at a position correspondning to position 112 of SEQ ID NO: 76 and / or a threonine at a position correspondning to position 198 of SEQ ID NO: 76. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 127 of SEQ ID NO: 76, a leucine at a position correspondning to position 136 of SEQ ID NO: 76, a valine at a position corresponding to position 138 of SEQ ID NO: 76, a leucine at a position correspondning to position 197 of SEQ ID NO: 76, a valine at a position correspondning to position 206 of SEQ ID NO: 76 and / or a tryptophan at a position correspondning to position 208 of SEQ ID NO: 76. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The Lactobacillus sp. carbonic anhydrase of SEQ ID NO: 79 contains key amino acid residues that may be important for activity (See alignment in Figure 44). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 79, 81, and / or 98 of SEQ ID NO: 79. In another embodiment, the carbonic anhydrase contains a glutamic acid at a position correspondning to position 85 of SEQ ID NO: 79 and / or a threonine at a position correspondning to position 163 of SEQ ID NO: 79. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 100 of SEQ ID NO: 79, a valine at a position corresponding to position 110 of SEQ ID NO: 79, a leucine at a position correspondning to position 162 of SEQ ID NO: 79, a valine at a position correspondning to position 183 of SEQ ID NO: 2 and / or a tryptophan at a position correspondning to position 171 of SEQ ID NO: 79. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 81 contains key amino acid residues that may be important for activity (See alignment in Figure 45). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 95, 97, and / or 114 of SEQ ID NO: 81. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 30 and / or 185 of SEQ ID NO: 81. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 11 of SEQ ID NO: 81, a histidine at a position corresponding to position 78 68 of SEQ ID NO: 81, a glutamic acid ata position correspondning to position 101 of SEQ ID NO: 81 and / or a threonine at a position correspondning to position 181 of SEQ ID NO: 81. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 116 of SEQ ID NO: 81, a leucine ata position correspondning to position 124 of SEQ ID NO: 81, a valine at a position corresponding to position 126 of SEQ ID NO: 81, a leucine at a position correspondning to position 180 of SEQ ID NO: 81, a valine at a position correspondning to position 189 of SEQ ID NO: 81 and / or a tryptophan at a position correspondning to position 191 of SEQ ID NO: 81. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. The carbonic anhydrase of SEQ ID NO: 83 contains key amino acid residues that may be important for activity (See alignment in Figure 46). Accordingly, in one embodiment of the present invention, the carbonic anhydrase contains a histidine residue at position(s) corresponsding to position 88, 90, and / or 107 of SEQ ID NO: 83. In another embodiment the carbonic anhydrase contains a cysteine residue at position(s) corresponding to position 25 and / or 180 of SEQ ID NO: 83. In another embodiment, the carbonic anhydrase contains a tyrosine at a position corresponding to position 6 of SEQ ID NO: 83, a histidine at a position corresponding to position 63 of SEQ ID NO: 83, a glutamic acid at a position correspondning to position 94 of SEQ ID NO: 83 and / or a threonine at a position correspondning to position 176 of SEQ ID NO: 83. Preferably, at least one of the proton shuttle positions are present, more preferably at least two proton shuttle positions are present, more preferably at least three proton shuttle positions are present and most preferably all the proton shuttle positions are present in the carbonic anhydrase. In another embodiment, the carbonic anhydrase contains a valine at a position corresponding to position 109 of SEQ ID NO: 83, a leucine at a position correspondning to position 117 of SEQ ID NO: 83, a valine at a position corresponding to position 119 of SEQ ID NO: 83, a leucine at a position correspondning to position 175 of SEQ ID NO: 83, a valine at a position correspondning to position 184 of SEQ ID NO: 83 and / or a tryptophan at a position correspondning to position 186 of SEQ ID NO: 83. Preferably, at least one of the residues responsible for CO2 binding is present, more preferably at least two, at least three, at least four, at least five, or all six residues. Additional guidance on the structure-activity relationship for the skilled artisan can be found in other published x-ray crystallography studies known in the art, e.g., the carbonic anhydrase of SEQ ID NO: 2 of PCT / US2023 / 081794 (Fredslund et al., 2018, Enzyme Microb. Technol. 114: 48-54). Additionally, structure-activity can be deciphered with the aid of the highly accurate neural network-based modelling program of AlphaFold (Jumper et al., Nature, 596: 583-589 (2021)). AlphaFold is a computational method for predicting the three-dimensional structure of a 79 polypeptide from its amino acid sequence. Predicted structures for millions of polypeptides deposited in the UniProt database have been deposited in the AlphaFold Protein Structure Database, using the AlphaFold Monomer v2.0 model (Varadi et al., Nucleic Acids Research, 50: D439-D444 (2021)). In the AlphaFold Protein Structure Database, the three-dimensional structure of a polypeptide can be obtained by searching for the UniProt accession number of the polypeptide. In addition to the many three-dimensional structures that are already publicly available, code is available for reproducing and predicting structures of new polypeptides at source code repositories. For the purposes of the present invention, the relatedness between the three-dimensional structure of two polypeptides is described by the parameter “structural similarity”. A threedimensional structure of any polypeptide may be obtained experimentally via, e.g., X-ray crystallography or using in silico methods such as AlphaFold (vide supra). The structural similarity between three-dimensional structures may then be determined by the TM-score, which is calculated using the following general formula (Zhang & Skolnick, Proteins, 57:702-710 (2004)): TM-score = Max where Ln is the length of the native structure, Lt is the length of the aligned residues to the template structure, dj is the distance between the ith pair of aligned residues and do is a scale to normalize the match difference. ‘Max’ denotes the maximum value after optimal spatial superposition. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 79, 81, 83, and 85, wherein the three dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 2, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 4, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 6, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 8, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 10, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 12, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 14, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 16, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 18, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 20, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 22, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 24, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 26, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 28, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 30, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 32, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 34, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 36, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 38, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 40, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at 83 least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 42, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 44, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 46, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 48, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 50, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 52, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, 84 at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 54, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 56, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 58, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 60, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 62, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 64, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 66, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 68, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 70, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 72, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 74, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 76, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 79, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at 86 least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 81, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 83, wherein the three-dimensional structure is calculated by Alphafold. In one embodiment, the carbonic anhydrase has a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of SEQ ID NO: 85, wherein the three-dimensional structure is calculated by Alphafold. Variants can be prepared using any mutagenesis procedure known in the art, such as site-directed mutagenesis, synthetic gene construction, semi-synthetic gene construction, random mutagenesis, shuffling, etc. Site-directed mutagenesis is a technique in which one or more mutations are introduced at one or more defined sites in a polynucleotide encoding the parent polypeptide. Site-directed mutagenesis can be accomplished in vitro by PCR involving the use of oligonucleotide primers containing the desired mutation. Site-directed mutagenesis can also be performed in vitro by cassette mutagenesis involving the cleavage by a restriction enzyme at a site in the plasmid comprising a polynucleotide encoding the parent and subsequent ligation of an oligonucleotide containing the mutation in the polynucleotide. Usually the restriction enzyme that digests the plasmid and the oligonucleotide is the same, permitting sticky ends of the plasmid and the insert to ligate to one another. See, e.g., Scherer and Davis, 1979, Proc. Natl. Acad. Sci. USA 7Q: 4949-4955; and Barton etal., 1990, Nucleic Acids Res. 18: 7349-4966. Site-directed mutagenesis can also be accomplished in vivo by methods known in the art. See, e.g., US 2004 / 0171154; Storici etal., 2001, Nature Biotechnol. 19: 773-776; Kren etal., 1998, Nat. Med. 4: 285-290; and Calissano and Macino, 1996, Fungal Genet. Newslett. 43: 1516. Any site-directed mutagenesis procedure can be used in the present invention. There are many commercial kits available that can be used to prepare variants. Synthetic gene construction entails in vitro synthesis of a designed polynucleotide molecule to encode a polypeptide of interest. Gene synthesis can be performed utilizing a number of techniques, such as the multiplex microchip-based technology described by Tian etal., 2004, 87 Nature 432: 1050-1054, and similar technologies wherein oligonucleotides are synthesized and assembled upon photo-programmable microfluidic chips. Single or multiple amino acid substitutions, deletions, and / or insertions can be made and tested using known methods of mutagenesis, recombination, and / or shuffling, followed by a relevant screening procedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241: 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156; WO 95 / 17413; or WO 95 / 22625. Other methods that can be used include error-prone PCR, phage display (e.g., Lowman eta!., 1991, Biochemistry30: 10832-10837; US 5,223,409; WO 92 / 06204), and region-directed mutagenesis (Derbyshire etal., 1986, Gene 46: 145; Ner et al., 1988, DNA 7: 127). Mutagenesis / shuffling methods can be combined with high-throughput, automated screening methods to detect activity of cloned, mutagenized polypeptides expressed by host cells (Ness etal., 1999, Nature Biotechnology 17: 893-896). Mutagenized DNA molecules that encode active polypeptides can be recovered from the host cells and rapidly sequenced using standard methods in the art. These methods allow the rapid determination of the importance of individual amino acid residues in a polypeptide. Semi-synthetic gene construction is accomplished by combining aspects of synthetic gene construction, and / or site-directed mutagenesis, and / or random mutagenesis, and / or shuffling. Semi-synthetic construction is typified by a process utilizing polynucleotide fragments that are synthesized, in combination with PCR techniques. Defined regions of genes may thus be synthesized de novo, while other regions may be amplified using site-specific mutagenic primers, while yet other regions may be subjected to error-prone PCR or non-error prone PCR amplification. Polynucleotide subsequences may then be shuffled. In one embodiment, the carbonic anhydrase has improved thermostability compared to the compared to carbonic anhyrases known in the art when tested under the same conditions (e.g., using an assay described in WO2018 / 017792, e.g., after incubation for the given time in 1 M NaHCOs buffer at pH 8 at the given elevated temperature). In one embodiment, the carbonic anhydrases are cablable of maintaining a residual activity of at least 30%, preferably above 40%, more preferably above 50%, more preferably above 60%, even more preferably above 70%, most preferably above 80%, most preferably above 85%, most preferably above 90%, most preferably above 95%, and even most preferably the residual activity is unchanged after incubation in 1 M NaHCOs buffer pH 8 at temperatures above 45 °C, preferably above 50 °C, above 55 °C, above 60 °C, above 65 °C, more preferably above 70 °C, most preferably above 80 °C, most preferably above 90 °C, most preferably above 100 °C, most preferably above 105 °C and even most preferably above 110 °C for at least 15 minutes, preferably for at least 2 hours, more preferably for at least 24 hours, more preferably for at least 7 days, more preferably for at least 10 days, even more preferably for at least 14 days, most preferably for at least 30 days, even most preferably for at least 50 days at the elevated temperature. In one embodiment, the carbonic anhydrase maintains at least 50% residual activity in 30% methyldiethanolamine (MDEA) at 85°C after five days. In one embodiment, the carbonic anhydrase maintains at least 85% activity when incubated for 15 minutes in 1M NaHCOs solution (approximately pH 8-10) in the temperature range 25-90°C. In one embodiment, the carbonic anhydrase maintains full activity at 50°C over the pH range 4-11 for one day. In one embodiment, the carbonic anhydrase maintains more than 50% activity over the pH range 4-11 after 10 days at 50°C. The polypeptide may be a fusion polypeptide. In an aspect, the polypeptide is isolated. In another aspect, the polypeptide is purified. Sources of Polypeptides Having Carbonic Anhydrase Activity A polypeptide having carbonic anhydrase activity of the present invention may be obtained from microorganisms of any genus. For purposes of the present invention, the term “obtained from” as used herein in connection with a given source shall mean that the polypeptide encoded by a polynucleotide is produced by the source or by a strain in which the polynucleotide of the invention has been inserted. In one aspect, the polypeptide obtained from a given source is secreted extracellularly. In one aspect, the carboninc anhydrase is a Endozoicomonas carbonic anhydrase, e.g., a carbonic anhydrase from Endozoicomonas arenosclerae or Endozoicomonas numazuensis, such as the carbonic anhydrase of SEQ ID NO: 2 or 6. In another aspect, the carboninc anhydrase is a Achromatium carbonic anhydrase, e.g., the Achromatium carbonic anhydrase of SEQ ID NO: 4. In another aspect, the carboninc anhydrase is a Thiorhodococcus carbonic anhydrase, e.g., a carbonic anhydrase from Thiorhodococcus drewsii, such as the carbonic anhydrase of SEQ ID NO: 8. In another aspect, the carboninc anhydrase is a Aquificales carbonic anhydrase, e.g., a carbonic anhydrase from Aquificales bacterium, such as the carbonic anhydrase of SEQ ID NO: 14. In another aspect, the carboninc anhydrase is a Trichophaea carbonic anhydrase, e.g., a carbonic anhydrase from Trichophaea saccata, such as the carbonic anhydrase of SEQ ID NO: 74. In another aspect, the carboninc anhydrase is a Eleutherascus carbonic anhydrase, e.g., a carbonic anhydrase from Eleutherascus tuberculatus, such as the carbonic anhydrase of SEQ ID NO: 76. In another aspect, the carboninc anhydrase is a Lactobacillus sp. carbonic anhydrase, such as the carbonic anhydrase of SEQ ID NO: 79. It will be understood that for the aforementioned species, the invention encompasses both the perfect and imperfect states, and other taxonomic equivalents, e.g., anamorphs, regardless of the species name by which they are known. Those skilled in the art will readily recognize the identity of appropriate equivalents. 5          The polypeptides may be identified and obtained from other sources including microorganisms isolated from nature (e.g., soil, composts, water, etc.) or DNA samples obtained directly from natural materials (e.g., soil, composts, water, etc.) using the above-mentioned probes. Techniques for isolating microorganisms and DNA directly from natural habitats are well known in the art. A polynucleotide encoding the polypeptide may then be obtained by similarly 10 screening a genomic DNA, metagenomic DNA or cDNA library of another microorganism or mixed DNA sample. Once a polynucleotide encoding a polypeptide has been detected with the probe(s), the polynucleotide can be isolated or cloned by utilizing techniques that are known to those of ordinary skill in the art (see, e.g., Davis etal., 2012, Basic Methods in Molecular Biology, Elsevier). 15 Polynucleotides The present invention also relates to polynucleotides encoding a polypeptide of the present invention, as described herein. The polynucleotide may be a genomic DNA, a cDNA, a synthetic DNA, a synthetic RNA, 20 a mRNA, or a combination thereof. The polynucleotide may be cloned from a strain of Endozoicomonas, Achromatium, Thiorhodococcus, Aquificales, Trichophaea, Eleutherascus or a related organism and thus, for example, may be a polynucleotide sequence encoding a variant of the carbonic anhydrase of the invention. In an embodiment, the polynucleotide is a subsequence encoding a fragment having 25 carbonic anhydrase of the present invention. In an aspect, the subsequence contains at least 85%, 90%, or 95% nucleotides of any one of SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 78, 80, 82, and 84. In one embodiment the polynucleotide encoding the polypeptide of the present invention 30 is isolated from a Endozoicomonas, Achromatium, Thiorhodococcus, Aquificales, Trichophaea, Eleutherascus or Lactobacillus cell. The polynucleotide may also be mutated by introduction of nucleotide substitutions that do not result in a change in the amino acid sequence of the polypeptide, but which correspond to the codon usage of the host organism intended for production of the enzyme, or by introduction 35 of nucleotide substitutions that may give rise to a different amino acid sequence. For a general description of nucleotide substitution, see, e.g., Ford et al., 1991, Protein Expression and Purification 2: 95-107. In an aspect, the polynucleotide is isolated. In another aspect, the polynucleotide is purified. Nucleic Acid Constructs The present invention also relates to nucleic acid constructs comprising a polynucleotide 5 of the present invention, wherein the polynucleotide is operably linked to one or more control sequences that direct the expression of the coding sequence in a suitable host cell under conditions compatible with the control sequences. The polynucleotide may be manipulated in a variety of ways to provide for expression of the polypeptide. Manipulation of the polynucleotide prior to its insertion into a vector may be 10 desirable or necessary depending on the expression vector. Techniques for modifying polynucleotides utilizing recombinant DNA methods are well known in the art. Promoters The control sequence may be a promoter, a polynucleotide that is recognized by a host 15 cell for expression of a polynucleotide encoding a polypeptide of the present invention. The promoter contains transcriptional control sequences that mediate the expression of the polypeptide. The promoter may be any polynucleotide that shows transcriptional activity in the host cell including mutant, truncated, and hybrid promoters, and may be obtained from genes encoding extracellular or intracellular polypeptides either homologous or heterologous to the host 20 cell. Examples of suitable promoters for directing transcription of the polynucleotide of the present invention in a bacterial host cell are described in Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Lab., NY, Davis et al., 2012, supra, and Song eta!., 2016, PLOS One 11(7): eO158447. 25           Examples of suitable promoters for directing transcription of the polynucleotide of the present invention in a filamentous fungal host cell are promoters obtained from Aspergillus, Fusarium, Rhizomucor and Trichoderma cells, such as the promoters described in Mukherjee et al., 2013, “Trichoderma: Biology and Applications”, and by Schmoll and Dattenbdck, 2016, “Gene Expression Systems in Fungi: Advancements and Applications”, Fungal Biology. 30          For expression in a yeast host, examples of useful promoters are described by Smolke et al., 2018, “Synthetic Biology: Parts, Devices and Applications” (Chapter 6: Constitutive and Regulated Promoters in Yeast: How to Design and Make Use of Promoters in S. cerevisiae), and by Schmoll and Dattenbdck, 2016, “Gene Expression Systems in Fungi: Advancements and Applications”, Fungal Biology. 35 Terminators The control sequence may also be a transcription terminator, which is recognized by a host cell to terminate transcription. The terminator is operably linked to the 3’-terminus of the polynucleotide encoding the polypeptide. Any terminator that is functional in the host cell may be used in the present invention. Preferred terminators for bacterial host cells may be obtained from the genes for Bacillus clausii alkaline protease (aprIT), Bacillus licheniformis alpha-amylase (amyL), and Escherichia coli ribosomal RNA (rrnB). Preferred terminators for filamentous fungal host cells may be obtained from Aspergillus or Trichoderma species, such as obtained from the genes for Aspergillus niger glucoamylase, Trichoderma reesei beta-glucosidase, Trichoderma reesei cellobiohydrolase I, and Trichoderma reesei endoglucanase I, such as the terminators described in Mukherjee et al., 2013, “Trichoderma: Biology and Applications”, and by Schmoll and Dattenbock, 2016, “Gene Expression Systems in Fungi: Advancements and Applications”, Fungal Biology. Preferred terminators for yeast host cells may be obtained from the genes for Saccharomyces cerevisiae enolase, Saccharomyces cerevisiae cytochrome C (CYC1), and Saccharomyces cerevisiae glyceraldehyde-3-phosphate dehydrogenase. Other useful terminators for yeast host cells are described by Romanos et al., 1992, Yeast 8: 423-488. mRNA Stabilizers The control sequence may also be an mRNA stabilizer region downstream of a promoter and upstream of the coding sequence of a gene which increases expression of the gene. Examples of suitable mRNA stabilizer regions are obtained from a Bacillus thuringiensis crylllA gene (WO 94 / 25612) and a Bacillus subtilis SP82 gene (Hue etal., 1995, J. Bacteriol. 177: 3465-3471). Examples of mRNA stabilizer regions for fungal cells are described in Geisberg et al., 2014, Cell 156(4): 812-824, and in Morozov etal., 2006, Eukaryotic Cell 5(11): 1838-1846. Leader Sequences The control sequence may also be a leader, a non-translated region of an mRNA that is important for translation by the host cell. The leader is operably linked to the 5’-terminus of the polynucleotide encoding the polypeptide. Any leader that is functional in the host cell may be used. Suitable leaders for bacterial host cells are described by Hambraeus et al., 2000, Microbiology 146(12): 3051-3059, and by Kaberdin and Blasi, 2006, FEMS Microbiol. Rev. 30(6): 967-979. Preferred leaders for filamentous fungal host cells may be obtained from the genes for Aspergillus oryzae TAKA amylase and Aspergillus nidulans triose phosphate isomerase. Suitable leaders for yeast host cells may be obtained from the genes for Saccharomyces cerevisiae enolase (ENO-1), Saccharomyces cerevisiae 3-phosphoglycerate kinase, Saccharomyces cerevisiae alpha-factor, and Saccharomyces cerevisiae alcohol dehydrogenase / glyceraldehyde-3-phosphate dehydrogenase (ADH2 / GAP). Polyadenylation Sequences The control sequence may also be a polyadenylation sequence, a sequence operably linked to the 3’-terminus of the polynucleotide which, when transcribed, is recognized by the host cell as a signal to add polyadenosine residues to transcribed mRNA. Any polyadenylation sequence that is functional in the host cell may be used. Preferred polyadenylation sequences for filamentous fungal host cells are obtained from the genes for Aspergillus nidulans anthranilate synthase, Aspergillus niger glucoamylase, Aspergillus niger alpha-glucosidase, Aspergillus oryzae TAKA amylase, and Fusarium oxysporum trypsin-like protease. Useful polyadenylation sequences for yeast host cells are described by Guo and Sherman, 1995, Mol. Cellular Biol. 15: 5983-5990. Signal Peptides The control sequence may also be a signal peptide coding region that encodes a signal peptide linked to the N-terminus of a polypeptide and directs the polypeptide into the cell’s secretory pathway. The 5’-end of the coding sequence of the polynucleotide may inherently contain a signal peptide coding sequence naturally linked in translation reading frame with the segment of the coding sequence that encodes the polypeptide. Alternatively, the 5’-end of the coding sequence may contain a signal peptide coding sequence that is heterologous to the coding sequence. A heterologous signal peptide coding sequence may be required where the coding sequence does not naturally contain a signal peptide coding sequence. Alternatively, a heterologous signal peptide coding sequence may simply replace the natural signal peptide coding sequence to enhance secretion of the polypeptide. Any signal peptide coding sequence that directs the expressed polypeptide into the secretory pathway of a host cell may be used. Effective signal peptide coding sequences for bacterial host cells are the signal peptide coding sequences obtained from the genes for Bacillus NCIB 11837 maltogenic amylase, Bacillus licheniformis subtilisin, Bacillus licheniformis beta-lactamase, Bacillus stearothermophilus alphaamylase, Bacillus stearothermophilus neutral proteases (nprT, nprS, nprM), and Bacillus subtilis prsA. Further signal peptides are described by Freudl, 2018, Microbial Cell Factories 17: 52. Effective signal peptide coding sequences for filamentous fungal host cells are the signal peptide coding sequences obtained from the genes for Aspergillus niger neutral amylase, Aspergillus niger glucoamylase, Aspergillus oryzae TAKA amylase, Humicola insolens cellulase, Humicola insolens endoglucanase V, Humicola lanuginosa lipase, and Rhizomucor miehei aspartic proteinase, such as the signal peptide described by Xu et al., 2018, Biotechnology Letters 40: 949-955 WO 2025 / 168806                                   PCT / EP2025 / 053303 Useful signal peptides for yeast host cells are obtained from the genes for Saccharomyces cerevisiae alpha-factor and Saccharomyces cerevisiae invertase. Other useful signal peptide coding sequences are described by Romanos et al., 1992, supra. Propeptides The control sequence may also be a propeptide coding sequence that encodes a propeptide positioned at the N-terminus of a polypeptide. The resultant polypeptide is known as a proenzyme or propolypeptide (or a zymogen in some cases). A propolypeptide is generally inactive and can be converted to an active polypeptide by catalytic or autocatalytic cleavage of the propeptide from the propolypeptide. The propeptide coding sequence may be obtained from the genes for Bacillus subtilis alkaline protease (aprE), Bacillus subtilis neutral protease (nprT), Myceliophthora thermophila laccase (WO 95 / 33836), Rhizomucor miehei aspartic proteinase, and Saccharomyces cerevisiae alpha-factor. Where both signal peptide and propeptide sequences are present, the propeptide sequence is positioned next to the N-terminus of a polypeptide and the signal peptide sequence is positioned next to the N-terminus of the propeptide sequence. Additionally or alternatively, when both signal peptide and propeptide sequences are present, the polypeptide may comprise only a part of the signal peptide sequence and / or only a part of the propeptide sequence. Alternatively, the final or isolated polypeptide may comprise a mixture of mature polypeptides and polypeptides which comprise, either partly or in full length, a propeptide sequence and / or a signal peptide sequence. Regulatory Sequences It may also be desirable to add regulatory sequences that regulate expression of the polypeptide relative to the growth of the host cell. Examples of regulatory sequences are those that cause expression of the gene to be turned on or off in response to a chemical or physical stimulus, including the presence of a regulatory compound. Regulatory sequences in prokaryotic systems include the lac, tac, and trp operator systems. In yeast, the ADH2 system or GAL1 system may be used. In filamentous fungi, the Aspergillus niger glucoamylase promoter, Aspergillus oryzae TAKA alpha-amylase promoter, and Aspergillus oryzae glucoamylase promoter, Trichoderma reesei cellobiohydrolase I promoter, and Trichoderma reesei cellobiohydrolase II promoter may be used. Other examples of regulatory sequences are those that allow for gene amplification. In fungal systems, these regulatory sequences include the dihydrofolate reductase gene that is amplified in the presence of methotrexate, and the metallothionein genes that are amplified with heavy metals. Transcription Factors The control sequence may also be a transcription factor, a polynucleotide encoding a polynucleotide-specific DNA-binding polypeptide that controls the rate of the transcription of genetic information from DNA to mRNA by binding to a specific polynucleotide sequence. The transcription factor may function alone and / or together with one or more other polypeptides or transcription factors in a complex by promoting or blocking the recruitment of RNA polymerase. Transcription factors are characterized by comprising at least one DNA-binding domain which often attaches to a specific DNA sequence adjacent to the genetic elements which are regulated by the transcription factor. The transcription factor may regulate the expression of a protein of interest either directly, i.e., by activating the transcription of the gene encoding the protein of interest by binding to its promoter, or indirectly, i.e., by activating the transcription of a further transcription factor which regulates the transcription of the gene encoding the protein of interest, such as by binding to the promoter of the further transcription factor. Suitable transcription factors for fungal host cells are described in WO 2017 / 144177. Suitable transcription factors for prokaryotic host cells are described in Seshasayee etal., 2011, Subcellular Biochemistry 52: 723, as well in Balleza etal., 2009, FEMS Microbiol. Rev. 33(1): 133-151. Expression Vectors The present invention also relates to recombinant expression vectors comprising a polynucleotide of the present invention, a promoter, and transcriptional and translational stop signals. The various nucleotide and control sequences may be joined together to produce a recombinant expression vector that may include one or more convenient restriction sites to allow for insertion or substitution of the polynucleotide encoding the polypeptide at such sites. Alternatively, the polynucleotide may be expressed by inserting the polynucleotide or a nucleic acid construct comprising the polynucleotide into an appropriate vector for expression. In creating the expression vector, the coding sequence is located in the vector so that the coding sequence is operably linked with the appropriate control sequences for expression. The recombinant expression vector may be any vector (e.g., a plasmid or virus) that can be conveniently subjected to recombinant DNA procedures and can bring about expression of the polynucleotide. The choice of the vector will typically depend on the compatibility of the vector with the host cell into which the vector is to be introduced. The vector may be a linear or closed circular plasmid. The vector may be an autonomously replicating vector, i.e., a vector that exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g., a plasmid, an extrachromosomal element, a minichromosome, or an artificial chromosome. The vector may contain any means for assuring self-replication. Alternatively, the vector may be one that, when introduced into the host cell, is integrated into the genome and replicated together with the chromosome(s) into which it has been integrated. Furthermore, a single vector or plasmid or two or more vectors or plasmids that together contain the total DNA to be introduced into the genome of the host cell, or a transposon, may be used. The vector preferably contains one or more selectable markers that permit easy selection of transformed, transfected, transduced, or the like cells. A selectable marker is a gene the product of which provides for biocide or viral resistance, resistance to heavy metals, prototrophy to auxotrophs, and the like. The vector preferably contains at least one element that permits integration of the vector into the host cell's genome or autonomous replication of the vector in the cell independent of the genome. For integration into the host cell genome, the vector may rely on the polynucleotide’s sequence encoding the polypeptide or any other element of the vector for integration into the genome by homologous recombination, such as homology-directed repair (HDR), or non-homologous recombination, such as non-homologous end-joining (NHEJ). For autonomous replication, the vector may further comprise an origin of replication enabling the vector to replicate autonomously in the host cell in question. The origin of replication may be any plasmid replicator mediating autonomous replication that functions in a cell. The term “origin of replication” or “plasmid replicator” means a polynucleotide that enables a plasmid or vector to replicate in vivo. More than one copy of a polynucleotide of the present invention may be inserted into a host cell to increase production of a polypeptide. For example, 2 or 3 or 4 or 5 or more copies are inserted into a host cell. An increase in the copy number of the polynucleotide can be obtained by integrating at least one additional copy of the sequence into the host cell genome or by including an amplifiable selectable marker gene with the polynucleotide where cells containing amplified copies of the selectable marker gene, and thereby additional copies of the polynucleotide, can be selected for by cultivating the cells in the presence of the appropriate selectable agent. Host Cells The present invention also relates to recombinant host cells, comprising a polynucleotide of the present invention operably linked to one or more control sequences that direct the production of a polypeptide of the present invention. A construct or vector comprising a polynucleotide is introduced into a host cell so that the construct or vector is maintained as a chromosomal integrant or as a self-replicating extra-chromosomal vector as described earlier. The choice of a host cell will to a large extent depend upon the gene encoding the polypeptide and its source. The polypeptide can be native or heterologous to the recombinant host cell. Also, at least one of the one or more control sequences can be heterologous to the polynucleotide encoding the polypeptide. The recombinant host cell may comprise a single copy, or at least two copies, e.g., three, four, five, or more copies of the polynucleotide of the present invention. The host cell may be any microbial cell useful in the recombinant production of a polypeptide of the present invention, e.g., a prokaryotic cell or a fungal cell. 5          The prokaryotic host cell may b...

Claims

1. A polypeptide having carbonic anhydrase activity, selected from the group consisting of:(a) a polypeptide having at least 60% sequence identity to any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 79, 81, 83, and 85;(b) a polypeptide encoded by a polynucleotide having at least 60% sequence identity to the coding sequence of any one of SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 78, 80, 82, and 84;(c) a polypeptide derived from any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 79, 81, 83, and 85 by having 1-30 alterations (e.g., substitutions, deletions and / or insertions at one or more positions, e.g., 1 or 2 or 3 or 4 or 5 or 6 or 7 or 8 or 9 or 10 or 11 or 12 or 13 or 14 or 15 or 16 or 17 or 18 or 19 or 20 or 21 or 22 or 23 or 24 or 25 or 26 or 27 or 28 or 29 or 30 alterations, in particular substitutions;(d) a polypeptide having a TM-score of at least 0.80, e.g., at least 0.85, at least 0.90, at least 0.905, at least 0.910, at least 0.915, at least 0.920, at least 0.925, at least 0.930, at least 0.935, at least 0.940, at least 0.945, at least 0.950, at least 0.955, at least 0.960, at least 0.965, at least 0.970, at least 0.975, at least 0.980, at least 0.985, at least 0.990, at least 0.995, or even 1.0, to the three-dimensional structure of the polypeptide of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 79, 81, 83, and 85, wherein the three-dimensional structure is calculated by Alphafold.(e) a polypeptide derived from the polypeptide of (a), (b), (c) or (d) wherein the N-and / or C-terminal end has been extended by addition of one or more amino acids; and(f) a fragment of the polypeptide of (a), (b), (c) or (d); wherein the polypeptide has carbonic anhydrase activity.

2. The polypeptide of claim 1, comprising, consisting essentially of, or consisting of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 79, 81, 83, and 85.

3. A composition comprising the polypeptide of claim 1 or 2.

4. A method of extracting carbon dioxide, the method comprising treating a carbon dioxidecontaining medium with a polypeptide of claim 1 or 2.

5. A bioreactor for extracting carbon dioxide, where said bioreactor comprises a polypeptide of claim 1 or 2.

6. A polynucleotide encoding the polypeptide of claim 1 or 2.

7. A nucleic acid construct or expression vector comprising the polynucleotide of claim 6, operably linked to one or more control sequences that direct the production of the polypeptide in an expression host.

8. A recombinant host cell comprising the nucleic acid construct or expression vector of claim 7.

9. A method of producing a polypeptide having carbonic anhydrase activity, comprising cultivating the recombinant host cell of claim 8 under conditions conducive for production of the polypeptide.

10. The method of claim 9 further comprising recovering the carbonic anhydrase.

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