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박테리아 헤모글로빈 공발현에 의한 Carbonic Anhydrase의 대장균 재조합 발현 향상Co-expression of Bacterial Hemoglobin Improves Recombinant Expression of Carbonic Anhydrase in Escherichia coli

Other Titles
Co-expression of Bacterial Hemoglobin Improves Recombinant Expression of Carbonic Anhydrase in Escherichia coli
Authors
조병훈차형준
Issue Date
Sep-2025
Publisher
한국생물공학회
Keywords
carbonic anhydrases; Escherichia coli; Vitreoscilla; hemoglobins; recombinant proteins
Citation
Korean Society for Biotechnology and Bioengineering Journal, v.40, no.3, pp 295 - 301
Pages
7
Indexed
KCI
Journal Title
Korean Society for Biotechnology and Bioengineering Journal
Volume
40
Number
3
Start Page
295
End Page
301
URI
https://scholarworks.gnu.ac.kr/handle/sw.gnu/81047
DOI
10.7841/ksbbj.2025.40.3.295
ISSN
1225-7117
2288-8268
Abstract
Carbonic anhydrase (CA) is a zinc-containing enzyme that catalyzes the CO2 hydration reaction. CA has gained much attention as a green and sustainable biocatalyst to accelerate CO2 capture and utilization. For industrial applications, it is desirable to reduce the enzyme production cost by improving the recombinant production of CA. Vitreoscilla hemoglobin (VHb) is a bacterial hemoglobin whose heterologous expression in Escherichia coli can improve cellular respiration and thereby recombinant protein production. In this study, Neisseria gonorrhoeae CA (NgCA) as a model CA was co-expressed with VHb in E. coli to improve the production of NgCA. When the VHb co-expression was controlled by the hypoxia-inducible Nar promoter, no visible VHb expression nor improvement in NgCA production was observed. In contrast, the bicistronic expression of VHb along with NgCA by the isopropyl-β-D-thiogalactopyranoside-inducible Trc promoter improved the expression level of NgCA by 15%-18%. The activity of purified NgCA was not affected by the VHb co-expression. Thus, the VHb co-expression should have general use as an effective strategy to increase the bacterial production of industrially relevant CA enzymes.
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