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Updated: Jul 20, 2026
Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
Published on: January 6, 2015
Electrochemical screening of recombinant protein solubility in Escherichia coli using scanning electrochemical
Kuniaki Nagamine1, Shiho Onodera, Ai Kurihara
1Graduate School of Environmental Studies, Tohoku University, 6-6-11 Aramaki Aoba, Aoba-ku, Sendai 980-8579, Japan.
Abstract:
A microbial array chip with collagen gel spots entrapping living Escherichia coli (E. coli) DH5alpha was applied for the screening of recombinant protein solubilities. The alpha-fragment of beta-galactosidase (betaGal) was fused to the target protein, namely, maltose-binding protein (MBP), to monitor the solubility of MBP. Scanning electrochemical microscopy (SECM) was used to detect the release of p-aminophenol from E. coli cells catalyzed by intracellular betaGal. Comparison of the SECM-based method with the Western blotting-based method indicated that the current response obtained using SECM increased with an increase in the betaGal activity and therefore, with the soluble fraction of MBP in the host cells.
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