Increased expression level and catalytic activity of internally-duplicated carbonic anhydrase from Dunaliella species by reconstitution of two separate domains
- Authors
- Ki, Mi-Ran; Kanth, Bashistha Kumar; Min, Ki Ha; Lee, Jinwon; Pack, Seung Pil
- Issue Date
- 9월-2012
- Publisher
- ELSEVIER SCI LTD
- Keywords
- Carbonic anhydrase; Dunaliella species; Repeat domain; CO2 mineralization; Calcite
- Citation
- PROCESS BIOCHEMISTRY, v.47, no.9, pp.1423 - 1427
- Indexed
- SCIE
SCOPUS
- Journal Title
- PROCESS BIOCHEMISTRY
- Volume
- 47
- Number
- 9
- Start Page
- 1423
- End Page
- 1427
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/107588
- DOI
- 10.1016/j.procbio.2012.05.005
- ISSN
- 1359-5113
- Abstract
- Although internally-duplicated, alpha-type carbonic anhydrase (CA) from Dunaliella species (Dsp-CA) can be expressed in Escherichia coli system, the produced amount is not sufficient for practical application. Here, we demonstrated to express the N- and C-half CA domains of Dsp-CA as distinct proteins to increase the expression levels further. The purified N-half CA domain (Dsp-CA-n) showed very low detectable activities of esterase or CO2 hydratase. In contrast, the purified C-half CA domain (Dsp-CA-c) retained both activities, which were enhanced by the presence of Dsp-CA-n. The expression levels of both domains were increased by 2-5-fold as compared to that of Dsp-CA. The CA activity was successfully reconstituted by mixing the two domains, N- and C-half domains, and more activity level was achieved than dimeric intact CA. These results newly suggest that the produced amount and activity of a duplicated CA are enhanced successfully by expressing each half CA domain individually and in vitro reconstitution. (C) 2012 Elsevier Ltd. All rights reserved.
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