An improved method for purification of recombinant truncated heme oxygenase-1 by expanded bed adsorption and gel filtration

被引：2
|
作者：
Hu, Hong-Bo [1 ]
Wang, Wei [1 ]
Han, Ling [1 ]
Zhou, Wen-Pu [1 ]
Zhang, Xue-Hong [1 ]
机构：
[1] Shanghai Jiao Tong Univ, Coll Life Sci & Biotechnol, Key Lab Microbial Metab, Minist Educ, Shanghai 200240, Peoples R China
来源：
BIOPROCESS AND BIOSYSTEMS ENGINEERING | 2007年 / 30卷 / 02期
关键词：
expanded bed adsorption; gel filtration; heme oxygenase-1; purification;
D O I：
10.1007/s00449-006-0103-y
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Recombinant truncated human heme oxygenase-1 (hHO-1) expressed in Escherichia coli was efficiently separated and purified from feedstock by DEAE-ion exchange expanded bed adsorption. Protocol optimization of hHO-1 on DEAE adsorbent resulted in adsorption in 0 M NaCl and elution in 150 mM NaCl at a pH of 8.5. The active enzyme fractions separated from the expanded bed column were further purified by a Superdex 75 gel filtration step. The specific hHO-1 activity increased from 0.82 +/- 0.05 to 24.8 +/- 1.8 U/mg during the whole purification steps. The recovery and purification factor of truncated hHO-1 of the whole purification were 72.7 +/- 4.7 and 30.2 +/- 2.3%, respectively. This purification process can decrease the demand on the preparation of feedstock and simplify the purification process.
引用
收藏
页码：87 / 90
页数：4
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