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

被引:24
作者
Lee, Soo Youn [1 ]
Lee, Hyun Jeong [2 ]
Park, Jae-Min [3 ]
Lee, Jin Hyung [4 ]
Park, Jin-Soo [5 ]
Shin, Hwa Sung [6 ]
Kim, Yang-Hoon [3 ]
Min, Jiho [1 ,2 ]
机构
[1] Chonbuk Natl Univ, Dept Bioproc Engn, Jeonju 561756, South Korea
[2] Chonbuk Natl Univ, Grad Sch Semicond & Chem Engn, Jeonju 561756, South Korea
[3] Chungbuk Natl Univ, Dept Microbiol, Cheongju 361763, South Korea
[4] KICET, BioIT Convergence Ctr, Seoul 153801, South Korea
[5] Sangmyung Univ, Coll Engn, Dept Environm Engn, Cheonan 330720, Chungnam Prov, South Korea
[6] Inha Univ, Dept Biol Engn, Inchon 402751, South Korea
关键词
Hydrogen; HupSL hydrogeanse; Rhodobacter sphaeroides; Recombinant E. coli; EXPRESSION; GLUCOSE;
D O I
10.1016/j.ijhydene.2009.11.068
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
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 degrees C to 30 degrees 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. (C) 2009 Professor T. Nejat Veziroglu. Published by Elsevier Ltd. All rights reserved.
引用
收藏
页码:1112 / 1116
页数:5
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