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References from Deep-sea bacterial alpha carbonic anhydrase as an efficient biocatalyst for sustainable CO2 mineralization. Local targets link to admitted publications; unresolved targets remain external evidence.
Carbon dioxide as a pollutant: the risks on human health and the stability of the biosphere
10.1039/d5va00017c · 2025 · External reference
Zero- and negative-emissions fossil-fired power plants using CO2 capture by conventional aqueous amines
10.1016/j.ijggc.2021.103473 · 2021 · External reference
Corrosion and degradation in MEA based post-combustion CO2 capture
10.1016/j.ijggc.2015.12.028 · 2016 · External reference
10.1186/s40643-015-0074-4 · 2015 · Admitted local publication
Shape controlled ZIF-8 crystals for carbonic anhydrase immobilization to boost CO2 uptake into aqueous MDEA solution
10.1016/j.seppur.2023.123683 · 2023 · External reference
Recent applications of carbonic anhydrase and its mimics in CO2 capture and utilization technologies
10.1016/j.geoen.2025.213958 · 2025 · External reference
Immobilized carbonic anhydrase: preparation, characteristics and biotechnological applications
10.1007/s11274-018-2536-2 · 2018 · External reference
Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism
10.3389/fmolb.2023.1326633 · 2023 · External reference
Carbonic anhydrase for CO2 capture, conversion and utilization
10.1016/j.copbio.2021.12.003 · 2022 · External reference
Carbonic anhydrases: Different active sites, same metal selectivity rules
10.3390/molecules29091995 · 2024 · External reference
Activation of α-, β-, γ- δ-, ζ- and η- class of carbonic anhydrases with amines and amino acids: a review
10.1080/14756366.2019.1664501 · 2019 · External reference
Probing the surface of human carbonic anhydrase for clues towards the design of isoform specific inhibitors
10.1155/2015/453543 · 2015 · External reference
Expression, reconstruction and characterization of codon-optimized carbonic anhydrase from Hahellachejuensis for CO2 sequestration application
10.1007/s00449-012-0788-z · 2013 · External reference
The structure of a tetrameric α-carbonic anhydrase from Thermovibrioammonificans reveals a core formed around intermolecular disulfides that contribute to its thermostability
10.1107/s1399004714016526 · 2014 · External reference
Carbonic Anhydrases: versatile and useful biocatalysts in chemistry and biochemistry
10.3390/catal10091008 · 2020 · External reference
Comparison of carbonic cnhydrases for CO2 Sequestration
10.3390/ijms23020957 · 2022 · External reference
Halotolerant carbonic anhydrase with unusual N-terminal extension from marine Hydrogenovibrio marinus as novel biocatalyst for carbon sequestration under high-salt environments
10.1016/j.jcou.2018.05.030 · 2018 · External reference
Enzymes from extreme environments and their industrial applications
10.3389/fbioe.2015.00161 · 2015 · External reference
Emerging trends in environmental and industrial applications of marine carbonic anhydrase: a review
10.1007/s00449-021-02667-8 · 2022 · External reference
Marine ammonification and carbonic anhydrase activity induce rapid calcium carbonate precipitation
10.1016/j.gca.2018.09.018 · 2018 · External reference
An α-carbonic anhydrase from the thermophilic bacterium Sulphuri hydrogenibium azorense is the fastest enzyme known for the CO2 hydration reaction
10.1016/j.bmc.2012.09.047 · 2013 · External reference
Activation studies of the γ-carbonic anhydrases from the antarcticmarine bacteriaPseudoalteromonashaloplanktis and Colwelliapsychrerythraea with amino acids and amines
10.3390/md17040238 · 2019 · External reference
Crystal structure and active site engineering of a halophilic γ-carbonic anhydrase
10.3389/fmicb.2020.00742 · 2020 · External reference
Functional-based screening methods for detecting esterase and lipase activity againstmultiple substrates
10.1007/978-1-4939-8672-9_4 · 2018 · External reference
Cleavage of structural proteins during the assembly of the head of bacteriophage T4
10.1038/227680a0 · 1970 · External reference
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
10.1016/0003-2697(76)90527-3 · 1976 · External reference
Evidencing the role of carbonic anhydrase in the formation of carbonate minerals by bacterial strains isolated from extreme environments in Qatar
10.1016/j.heliyon.2022.e11151 · 2022 · External reference
Electrometric and colorimetric determination of carbonic anhydrase
10.1016/s0021-9258(18)51011-5 · 1948 · External reference
Engineering of Thermovibrioammonificans carbonic anhydrase mutants with increased thermostability
10.1016/j.jcou.2019.11.015 · 2020 · External reference
The clustalomega multiple mlignmentpackage
10.1007/978-1-0716-1036-7_1 · 2021 · External reference
I-TASSER: a unified platform for automated protein structure and function prediction
10.1038/nprot.2010.5 · 2010 · External reference
SignalP 6.0 predicts all five types of signal peptides using protein language models
10.1038/s41587-021-01156-3 · 2022 · External reference
Exhaustive comparison and classification of ligand-binding surfaces in proteins
10.1002/pro.2329 · 2013 · External reference
AmberTools
10.1021/acs.jcim.3c01153 · 2023 · External reference
Genome sequence analysis of deep seaAspergillus sydowii BOBA1 and effect of high pressure on biodegradation of spent engine oil
10.1038/s41598-021-88525-9 · 2021 · External reference
Characterization of marine bacterial carbonic anhydrase and their CO2 sequestration abilities based on a soil microcosm
10.1080/10826068.2019.1633669 · 2019 · External reference
Exploration of the advantages of targeted isolation of deep-sea microorganisms and genetically engineered strains
10.1007/s11274-024-04177-7 · 2024 · External reference
The PSIPRED Protein Analysis Workbench: 20 years on
10.1093/nar/gkz297 · 2019 · External reference
Structure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimney
10.1016/j.enzmictec.2018.03.009 · 2018 · External reference
The prospective and potential of carbonic anhydrase for carbon dioxide sequestration: A critical review
10.1016/j.procbio.2019.08.018 · 2019 · External reference
The PROSITE database
10.1093/nar/gkj063 · 2006 · External reference
Carbonic anhydrase to boost CO2 sequestration: Improving carbon capture utilization and storage (CCUS)
10.1016/j.chemosphere.2022.134419 · 2022 · External reference
A new carbonic anhydrase identified in the Gram-negative bacterium (Chromohalobacter sp.) and the interaction of anions with the enzyme
10.1016/j.cbpc.2022.109290 · 2022 · External reference
Enzyme mediated transformation of CO2 into calcium carbonate using purified microbial carbonic anhydrase
10.1016/j.envres.2022.113538 · 2022 · External reference
Immobilization and characterization of carbonic anhydrase purified from E. coli MO1 and its influence on CO2 sequestration
10.1007/s11274-013-1343-z · 2013 · External reference
Purification and characterization of an extracellular carbonic anhydrase from Pseudomonas fragi
10.1016/j.procbio.2009.07.022 · 2009 · External reference
Characteristics of recombinant α-carbonic anhydrase of polyextremophilic bacterium Bacillus halodurans TSLV1
10.1016/j.ijbiomac.2016.05.026 · 2016 · External reference
Biochemical properties of a novel and highly thermostable bacterial α-carbonic anhydrase from Sulfurihydrogenibiumyellowstonense YO3AOP1
10.3109/14756366.2012.703185 · 2012 · External reference
Crystal Structure of a Highly Thermostable α-Carbonic Anhydrase from Persephonella marina EX-H1
10.14348/molcells.2019.0029 · 2019 · External reference
Biochemical characterization of a psychrophilic and halotolerant α-carbonic anhydrase from a deep-sea bacterium, Photobacterium profundum
10.3934/microbiol.2023028 · 2023 · External reference
Unresolved reference
2013 · External reference
Functional characterisation of a new halotolerant seawater active glycoside hydrolase family 6 cellobiohydrolase from a salt marsh
10.1038/s41598-024-53886-4 · 2024 · External reference
Molecular bases of protein halotolerance
10.1016/j.bbapap.2014.02.018 · 2014 · External reference
Rational engineering of a mesohalophilic carbonic anhydrase to an extreme halotolerant biocatalyst
10.1038/ncomms10278 · 2015 · External reference
Developing a hybrid carbonic anhydrase with exceptional high temperature and alkaline environments resistance for efficient CO2 capture from air
10.1016/j.jcou.2024.102912 · 2024 · External reference
Mineral carbonation using seawater for CO2 sequestration and utilization: A review
10.1016/j.seppur.2022.122855 · 2023 · External reference
Study of microalgae biofixation with bacteria carbonic anhydrase for carbon capture and utilization
10.3390/su162411196 · 2024 · External reference
The catalytic role of carbonic anhydrase in optimizing carbon fixation in microalgal cultures
2025 · External reference
Enhancement of microalgal carbon fixation via synergistic interactions with a facultative autotrophic bacterium Cytobacillus KQ-2
10.1016/j.biortech.2025.133310 · 2026 · External reference
Ancestral carbonic anhydrase with significantly enhanced stability and activity for CO2 capture and utilization
10.1016/j.biortech.2025.132054 · 2025 · External reference
Study of CO2 capture by seawater and its reinforcement
10.1016/j.energy.2018.09.066 · 2018 · External reference
CO2 capture with potassium carbonate solutions: A state-of-the-art review
10.1016/j.ijggc.2015.06.026 · 2015 · External reference
Sensitivity of water dynamics to biologically significant surfaces of monomeric insulin: role of topology and electrostatic interactions
10.1021/jp411136w · 2014 · External reference
A model of the pressure dependence of the enantioselectivity of Candida rugosalipase towards (+/-)-menthol
10.1110/ps.12301 · 2001 · External reference
Comparison and mechanism of CO2 sequestration by different carbonic anhydrase producing bacteria
10.1016/j.bej.2025.109812 · 2025 · External reference
Carbonic anhydrase-producing bacteria-mediated sandstone-CO2-brine interaction and its impact on carbon sequestration
10.1016/j.envres.2025.122801 · 2025 · External reference
Enhanced sequestration of carbon dioxide into calcium carbonate using pressure and a carbonic anhydrase from alkaliphilic Coleofasciculu schthonoplastes
10.1002/elsc.202100033 · 2022 · External reference
The influence and correlation analysis of environmental factors and saturation index on the calcium carbonate precipitation induced by carbonic anhydrase-producing bacteria
10.1016/j.procbio.2026.01.010 · 2026 · External reference
Biomineralization of carbon dioxide by carbonic anhydrase
10.1016/j.bcab.2023.102755 · 2023 · External reference
Understanding microbial biomineralization at the molecular level: recent advances
10.1007/s11274-024-04132-6 · 2024 · External reference
Novel bovine carbonic anhydrase encapsulated in a metal-organic framework: a new platform for biomimetic sequestration of CO2
10.1039/c9ra04603h · 2019 · External reference
Carbon composite beads for immobilization of carbonic anhydrase
10.1016/j.molcatb.2011.03.011 · 2011 · External reference
