Enhanced production of recombinant galactose oxidase from Fusarium graminearum in E. coli

被引：0
|
作者：
Withu Choosri
Regina Paukner
Petra Wührer
Dietmar Haltrich
Christian Leitner
机构：
[1] BOKU,Department of Food Sciences and Technology, Food Biotechnology Laboratory
[2] University of Natural Resources and Life Sciences,undefined
来源：
World Journal of Microbiology and Biotechnology | 2011年 / 27卷
关键词：
Galactose oxidase; Overexpression; Fermentation; Affinity chromatography;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
The gene gaoA encoding the copper-dependent enzyme galactose oxidase (GAO) from Fusarium graminearum PH-1 was cloned and successfully overexpressed in E. coli. Culture conditions for cultivations in shaken flasks were optimized, and optimal conditions were found to be double-strength LB medium, 0.5% lactose as inducer, and induction at the reduced temperature of 25°C. When using these cultivation conditions ~24 mg of active GAO could be produced in shaken flasks per litre medium. Addition of copper to the fermentation medium decreased the enzyme production significantly. The His-tagged recombinant enzyme could be purified conveniently with a single affinity chromatography step. The purified enzyme showed a single band on SDS–PAGE with an apparent molecular mass of 66 kDa and had kinetic properties similar to those of the fungal wild-type enzyme.
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页码：1349 / 1353
页数：4
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