Publisher DOI: 10.1002/elsc.202100033
Title: Enhanced sequestration of carbon dioxide into calcium carbonate using pressure and a carbonic anhydrase from alkaliphilic Coleofasciculus chthonoplastes
Language: English
Authors: Heuer, Jonas 
Kraus, Yasemin 
Vučak, Marijan 
Zeng, An-Ping  
Keywords: calcium carbonate;carbon dioxide;carbonic anhydrase;high pressure;sequestration
Issue Date: 2021
Source: Engineering in Life Sciences : (2021) (in press; CC BY 4.0)
Journal: Engineering in life sciences 
Abstract (english): 
CO2 in the atmosphere is a major contributor to global warming but at the same time it has the potential to be a carbon source for advanced biomanufacturing. To utilize CO2, carbonic anhydrase has been identified as a key enzyme. Furthermore, attempts have been made to accelerate the sequestration via pressure. This study aims to combine both approaches to achieve high sequestration rates. The carbonic anhydrase of the alkaliphilic cyanobacterium Coleofasciculus chthonoplastes (cahB1) and bovine carbonic anhydrase (BCA) are introduced into a high-pressure reactor to catalyze the hydration of CO2 at up to 20 bar. The reactor is filled with a CaCl2 solution. Due to the presence of Ca2+, the hydrated CO2 precipitates as CaCO3. The impact of the carbonic anhydrase is clearly visible at all pressures tested. At ambient pressure a CO2 sequestration rate of 243.68 kgCaCO3/m3 h for cahB1 was achieved compared to 150.41 kgCaCO3/m3 h without enzymes. At 20 bar the rates were 2682.88 and 2267.88 kgCaCO3/m3 h, respectively. The study shows the benefit of a combined CO2 sequestration process. To examinate the influence of the enzymes on the product formation, the precipitated CaCO3 was analyzed regarding the crystalline phase and morphology. An interchange of the crystalline phase from vaterite to calcite was observed and discussed.
URI: http://hdl.handle.net/11420/11070
ISSN: 1618-0240
Institute: Bioprozess- und Biosystemtechnik V-1 
Document Type: Article
Project: Protein Pressure Specific Activity Impact "Modulation der Reaktivität von Proteinen und Thermodynamik durch Druck" 
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