Carbonic anhydrase for CO2 capture, conversion and utilization

2022 ◽  
Vol 74 ◽  
pp. 230-240
Sachin Talekar ◽  
Byung Hoon Jo ◽  
Jonathan S Dordick ◽  
Jungbae Kim
2017 ◽  
Vol 114 ◽  
pp. 1434-1443 ◽  
Philip Loldrup Fosbøl ◽  
Jozsef Gaspar ◽  
Bjartur Jacobsen ◽  
Jens Glibstrup ◽  
Arne Gladis ◽  

2017 ◽  
Vol 5 (37) ◽  
pp. 19954-19962 ◽  
Yiming Zhang ◽  
Huixian Wang ◽  
Jindun Liu ◽  
Jingwei Hou ◽  
Yatao Zhang

In this work, carbonic anhydrase (CA) molecules were embedded into metal–organic frameworks (MOFs) via physical absorption and chemical bonds, which could overcome the enzymatic inactivation and the poor separation property of pristine MOF materials.

2018 ◽  
Vol 54 (52) ◽  
pp. 7239-7242 ◽  
Yanni Liu ◽  
Zhi Wang ◽  
Mengqi Shi ◽  
Nan Li ◽  
Song Zhao ◽  

Hydrophobic channels of ion-exchanged zeolite β imitate the function of the hydrophobic pocket in carbonic anhydrase.

2021 ◽  
pp. 134029
Hannaneh Rasouli ◽  
Ion Iliuta ◽  
Francis Bougie ◽  
Alain Garnier ◽  
Maria C. Iliuta

Ryohei Sato ◽  
Yutaka Amao

In order to establish carbon capture, utilization, and storage (CCUS) technology, we focused on the system consisting of two different biocatalysts (formate dehydrogenase from Candida boidinii; CbFDH and carbonic anhydrase...

2019 ◽  
Vol 21 (1) ◽  
pp. 103 ◽  
Byung Hoon Jo ◽  
In Seong Hwang

Carbonic anhydrase (CA) is a diffusion-controlled enzyme that rapidly catalyzes carbon dioxide (CO2) hydration. CA has been considered as a powerful and green catalyst for bioinspired CO2 capture and utilization (CCU). For successful industrial applications, it is necessary to expand the pool of thermostable CAs to meet the stability requirement under various operational conditions. In addition, high-level expression of thermostable CA is desirable for the economical production of the enzyme. In this study, a thermostable CA (tdCA) of Thermosulfurimonas dismutans isolated from a deep-sea hydrothermal vent was expressed in Escherichia coli and characterized in terms of expression level, solubility, activity and stability. tdCA showed higher solubility, activity, and stability compared to those of CA from Thermovibrio ammonificans, one of the most thermostable CAs, under low-salt aqueous conditions. tdCA was engineered for high-level expression by the introduction of a point mutation and periplasmic expression via the Sec-dependent pathway. The combined strategy resulted in a variant showing at least an 8.3-fold higher expression level compared to that of wild-type tdCA. The E. coli cells with the periplasmic tdCA variant were also investigated as an ultra-efficient whole-cell biocatalyst. The engineered bacterium displayed an 11.9-fold higher activity compared to that of the recently reported system with a halophilic CA. Collectively these results demonstrate that the highly expressed periplasmic tdCA variant, either in an isolated form or within a whole-cell platform, is a promising biocatalyst with high activity and stability for CCU applications.

2013 ◽  
Vol 53 (4) ◽  
pp. 271-277 ◽  
Maria Elena Russo ◽  
Giuseppe Olivieri ◽  
Clemente Capasso ◽  
Viviana De Luca ◽  
Antonio Marzocchella ◽  

2020 ◽  
Vol 21 (8) ◽  
pp. 2918
Aline M. de Castro ◽  
Elisabete Ferreira ◽  
Carla Portugal ◽  
Luisa A. Neves ◽  
João G. Crespo

The unprecedently high CO2 levels in the atmosphere evoke the urgent need for development of technologies for mitigation of its emissions. Among the alternatives, the biocatalytic route has been claimed as one of the most promising. In the present work, the carbonic anhydrase from bovine erythrocytes (BCA) was employed as a model enzyme for structural studies in an aqueous phase at alkaline pH, which is typical of large-scale absorption processes under operation. Circular dichroism (CD) analysis revealed a high enzymatic stability at pH 10 with a prominent decrease of the melting temperature above this value. The CO2 absorption capacity of the aqueous solutions were assessed by online monitoring of pressure decay in a stainless-steel cell, which indicated a better performance at pH 10 with a kinetic rate increase of up to 43%, as compared to non-biocatalytic conditions. Even low enzyme concentrations (0.2 mg g−1) proved to be sufficient to improve the overall CO2 capture process performance. The enzyme-enhanced approach of CO2 capture presents a high potential and should be further studied.

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