Bacterial hydrogen production in recombinant Escherichia coli harboring a HupSL hydrogenase isolated from Rhodobacter sphaeroides under anaerobic dark culture

In this study, recombinant plasmid was constructed to analyze the effect of hydrogen production on the expression HupSL hydrogenase isolated from Rhodobacter sphaeroides in Escherichia coli. Although most of recombinant HupSL hydrogenase was produced as inclusion bodies the solubility of the protein...

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Bibliographic Details
Published in:International journal of hydrogen energy 2010-02, Vol.35 (3), p.1112-1116
Main Authors: Lee, Soo Youn, Lee, Hyun Jeong, Park, Jae-Min, Lee, Jin Hyung, Park, Jin-Soo, Shin, Hwa Sung, Kim, Yang-Hoon, Min, Jiho
Format: Article
Language:English
Subjects:
Energy
Escherichia coli
HupSL hydrogeanse
Hydrogen
Recombinant E. coli
Rhodobacter sphaeroides
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Summary:In this study, recombinant plasmid was constructed to analyze the effect of hydrogen production on the expression HupSL hydrogenase isolated from Rhodobacter sphaeroides in Escherichia coli. Although most of recombinant HupSL hydrogenase was produced as inclusion bodies the solubility of the protein increased significantly when the expression temperature shifted from 37 °C to 30 °C. Hydrogen production by expression of HupSL hydrogenase from recombinant E. coli increased 20.9-fold compared to control E. coli and 218-fold compared to wild type R. sphaeroides under anaerobic dark condition. The results demonstrate that HupSL hydrogenase, consisting of small and large subunits of hydrogenase isolated from R. sphaeroides, increases hydrogen production in recombinant E. coli. In addition conditions for enhancing the activity of HupSL hydrogenase in E. coli were suggested and were used to increase bacterial hydrogen production.
ISSN:0360-3199
1879-3487
DOI:10.1016/j.ijhydene.2009.11.068