Expression and characterization of a codon-optimized alkaline-stable carbonic anhydrase from class="a-plus-plus">Aliivibrio salmonicida for CO_{class="a-plus-plus">2} sequestration applications

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• 作者：So-Young Jun ; Sung Ho Kim ; Bashista Kumar Kanth…
• 关键词：Carbonic anhydrase ; Codon optimization ; CO2 sequestration ; Aliivibrio salmonicida
• 刊名：Bioprocess and Biosystems Engineering
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：40
• 期：3
• 页码：413-421
• 全文大小：
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Biotechnology; Industrial and Production Engineering; Environmental Engineering/Biotechnology; Industrial Chemistry/Chemical Engineering; Food Science;
• 出版者：Springer Berlin Heidelberg
• ISSN：1615-7605
• 卷排序：40

文摘

The CO₂ mineralization process, accelerated by carbonic anhydrase (CA) was proposed for the efficient capture and storage of CO₂, the accumulation of which in the atmosphere is the main cause of global warming. Here, we characterize a highly stable form of the cloned CA from the Gram-negative marine bacterium Aliivibrio salmonicida, named ASCA that can promote CO₂ absorption in an alkaline solvent required for efficient carbon capture. We designed a mature form of ASCA (mASCA) using a codon optimization of ASCA gene and removal of ASCA signal peptide. mASCA was highly expressed (255 mg/L) with a molecular weight of approximately 26 kDa. The mASCA enzyme exhibited stable esterase activity within a temperature range of 10–60 °C and a pH range of 6–11. mASCA activity remained stable for 48 h at pH 10. We also investigated its inhibition profiles using inorganic anions, such as acetazolamide, sulfanilamide, iodide, nitrate, and azide. We also demonstrate that mASCA is capable of catalyzing the conversion of CO₂ to CaCO₃ (calcite form) in the presence of Ca2+. It should be noted that mASCA enzyme exhibits high production yield and sufficient stabilities against relatively high temperature and alkaline pH, which are required conditions for the development of more efficient enzymatic CCS systems.