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首页> 外文期刊>Bioprocess and Biosystems Engineering >An improved method for purification of recombinant truncated heme oxygenase-1 by expanded bed adsorption and gel filtration
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An improved method for purification of recombinant truncated heme oxygenase-1 by expanded bed adsorption and gel filtration

机译：一种通过扩展床吸附和凝胶过滤纯化重组截短的血红素加氧酶-1的方法

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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.
机译：大肠杆菌中表达的重组截短的人血红素加氧酶-1（hHO-1）通过DEAE离子交换膨胀床吸附从原料中有效分离和纯化。 hHO-1在DEAE吸附剂上的方案优化导致在0 M NaCl中吸附并在pH值为8.5的150 mM NaCl中洗脱。从膨胀床柱分离的活性酶馏分通过Superdex 75凝胶过滤步骤进一步纯化。在整个纯化步骤中，hHO-1的比活性从0.82±0.05增加到24.8±1.8 U / mg。整个纯化过程中截短的hHO-1的回收率和纯化因子分别为72.7±4.7和30.2±2.3％。该纯化过程可以减少对原料制备的需求并简化纯化过程。

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