Solubility enhancement of aggregation-prone heterologous proteins by fusion expression using stress-responsive <Emphasis Type="Italic">Escherichia coli</Emphasis>protein,RpoS |
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| Authors: | Jin-Seung Park Kyung-Yeon Han Jong-Ho Lee Jong-Am Song Keum-Young Ahn Hyuk-Seong Seo Sang-Jun Sim Seung-Wook Kim Jeewon Lee |
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| Institution: | (1) Department of Chemical and Biological Engineering, Korea University, Anam-Dong 5-1, Sungbuk-Ku, Seoul, 136-713, South Korea;(2) Department of Chemical Engineering, Sungkyunkwan University, Suwon, South Korea |
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| Abstract: | Background The most efficient method for enhancing solubility of recombinant proteins appears to use the fusion expression partners.
Although commercial fusion partners including maltose binding protein and glutathione-S-transferase have shown good performance in enhancing the solubility, they cannot be used for the proprietory production of
commercially value-added proteins and likely cannot serve as universal helpers to solve all protein solubility and folding
issues. Thus, novel fusion partners will continue to be developed through systematic investigations including proteome mining
presented in this study. |
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