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

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Bibliographic Details
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]
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Database:	Engineering Source

Description
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]
ISSN:	16157591
DOI:	10.1007/s00449-012-0788-z