Production of biohydrogen by heterologous expression of oxygen-tolerant Hydrogenovibrio marinus [NiFe]-hydrogenase in Escherichia coli
SCIE
SCOPUS
- Title
- Production of biohydrogen by heterologous expression of oxygen-tolerant Hydrogenovibrio marinus [NiFe]-hydrogenase in Escherichia coli
- Authors
- Kim, JYH; Jo, BH; Cha, HJ
- Date Issued
- 2011-09-20
- Publisher
- ELSEVIER SCIENCE BV
- Abstract
- Oxygen sensitivity of hydrogenase is a critical issue in efficient biological hydrogen production. In the present study, oxygen-tolerant [NiFe]-hydrogenase from the marine bacterium, Hydrogenovibrio marinus, was heterologously expressed in Escherichia coli, for the first time. Recombinant E. coli BL21 expressing H. marinus [NiFe]-hydrogenase actively produced hydrogen, but the parent strain did not. Recombinant H. marinus hydrogenase required both nickel and iron for biological activity. Compared to the recombinant E. coli [NiFe]-hydrogenase 1 described in our previous report, recombinant H. marinus [NiFe]-hydrogenase displayed 1.6- to 1.7-fold higher hydrogen production activity in vitro. Importantly, H. marinus [NiFe]hydrogenase exhibited relatively good oxygen tolerance in analyses involving changes of surface aeration and oxygen proportion within a gas mixture. Specifically, recombinant H. marinus [NiFe]-hydrogenase produced similar to 7-to 9-fold more hydrogen than did E. coli [NiFe]-hydrogenase 1 in a gaseous environment containing 5-10% (v/v) oxygen. In addition, purified H. marinus [NiFe]-hydrogenase displayed a hydrogen evolution activity of similar to 28.8 nmol H-2/(min mg protein) under normal aerobic purification conditions. Based on these results, we suggest that oxygen-tolerant H. marinus [NiFe]-hydrogenase can be employed for in vivo and in vitro biohydrogen production without requirement for strictly anaerobic facilities. (C) 2011 Elsevier B.V. All rights reserved.
- Keywords
- Biohydrogen; [NiFe]-hydrogenase; Oxygen-tolerance; Hydrogenovibrio marinus; Escherichia coli; NIFE-HYDROGENASE GENES; LOW-LEVEL H-2; THIOCAPSA-ROSEOPERSICINA; OXIDIZING BACTERIUM; SPECIFICITY; MATURATION; OXIDATION; CLONING; SITE; AIR
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/17078
- DOI
- 10.1016/J.JBIOTEC.2011.07.007
- ISSN
- 0168-1656
- Article Type
- Article
- Citation
- JOURNAL OF BIOTECHNOLOGY, vol. 155, no. 3, page. 312 - 319, 2011-09-20
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- There are no files associated with this item.
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