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Expression, reconstruction and characterization of codon-optimized carbonic anhydrase from Hahella chejuensis for CO sequestration application.

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Title: Expression, reconstruction and characterization of codon-optimized carbonic anhydrase from Hahella chejuensis for CO sequestration application.
Authors: Ki, Mi-Ran1, Min, Kiha1, Kanth, Bashistha1, Lee, Jinwon2 jinwonlee@sogang.ac.kr, Pack, Seung1 spack@korea.ac.kr
Source: Bioprocess & Biosystems Engineering. Mar2013, Vol. 36 Issue 3, p375-381. 7p.
Subjects: Carbonic anhydrase, Carbon sequestration, Escherichia coli, Foodborne diseases, Zinc
Abstract: The high production of functional carbonic anhydrase (CA) is required for practical CO sequestration application mediated by CA. Here, the synthetic gene based on Escherichia coli codon usage of new α-type CA (HC-aCA) of Hahella chejuensis, a Korea marine microorganism, was highly expressed in E. coli. We obtained a high yield of functional HC-aCA by denaturing/refolding process and incorporating zinc ion into its active site. The refolded HC-aCA displayed a half-deactivation temperature of 60 °C with maximal activity at 50 °C, and had high pH stability in alkali condition with maximal activity at pH 10.0. The esterase activity of HC-aCA almost doubled at high salt concentration ranging from 0.67 to 2.0 M NaCl. HC-aCA catalyzed the conversion of CO to CaCO as calcites form in the presence of Ca. The refolded HC-aCA could be a promising candidate for the development of efficient CA-based CO sequestration processes. [ABSTRACT FROM AUTHOR]
Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: The high production of functional carbonic anhydrase (CA) is required for practical CO sequestration application mediated by CA. Here, the synthetic gene based on Escherichia coli codon usage of new α-type CA (HC-aCA) of Hahella chejuensis, a Korea marine microorganism, was highly expressed in E. coli. We obtained a high yield of functional HC-aCA by denaturing/refolding process and incorporating zinc ion into its active site. The refolded HC-aCA displayed a half-deactivation temperature of 60 °C with maximal activity at 50 °C, and had high pH stability in alkali condition with maximal activity at pH 10.0. The esterase activity of HC-aCA almost doubled at high salt concentration ranging from 0.67 to 2.0 M NaCl. HC-aCA catalyzed the conversion of CO to CaCO as calcites form in the presence of Ca. The refolded HC-aCA could be a promising candidate for the development of efficient CA-based CO sequestration processes. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1007/s00449-012-0788-z
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        Text: English
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      – SubjectFull: Escherichia coli
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              Text: Mar2013
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