Biotechnology and Bioprocess Engineering:BBE

The Korean Society for Biotechnology and Bioengineering (한국생물공학회)
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The Soluble Expression of the Human Renin Binding Protein Using Fusion Partners: A Comparison of ubquitin, Thioredoxin, Maltose Binding Protein-and NusA

  • Lee, Chung (School of Chemical Engineering, and Institute of Molecular Biology and Genetics, Seoul National University) ;
  • Lee, Sun-Gu (School of Chemical Engineering, and Institute of Molecular Biology and Genetics, Seoul National University) ;
  • Saori Takahashi (Department of Bioengineering, Akita Research Institute of Food and Brewing) ;
  • Kim, Byung-Gee (School of Chemical Engineering, and Institute of Molecular Biology and Genetics, Seoul National University)
  • Published : 2003.04.01
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Abstract

human renin binding protein (hRnBp), showing N-acetylglucosamine-2-epimerase activity, was over-expressed in E. coli, but was mainly present as an inclusion body. To improve its solubility and activity, ubiquitin (Ub), thioredoxin (Trx), maltose binding protein (MBP) and NusA, were used as fusion partners. The comparative solubilities of the fusion proteins were, from most to least soluble: NusA, MBP, Trx, Ub. Only the MBP fusion did not significantly reduce the activity of hRnBp, but enhanced the stability. The Origami (DE3), permitting a more oxidative environment for the cytoplasm in E. coli; helped to increase its functional activity.

Keywords

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