期刊
JOURNAL OF BIOTECHNOLOGY
卷 155, 期 3, 页码 312-319出版社
ELSEVIER
DOI: 10.1016/j.jbiotec.2011.07.007
关键词
Biohydrogen; [NiFe]-hydrogenase; Oxygen-tolerance; Hydrogenovibrio marinus; Escherichia coli
资金
- Ministry of Education, Science and Technology, Korea [NRF-2009-0093214]
- Ministry of Land, Transport and Maritime Affairs, Korea
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.
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