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Electrochemical screening of recombinant protein solubility in Escherichia coli using scanning electrochemical microscopy (SECM)

✍ Scribed by Kuniaki Nagamine; Shiho Onodera; Ai Kurihara; Tomoyuki Yasukawa; Hitoshi Shiku; Ryutaro Asano; Izumi Kumagai; Tomokazu Matsue

Publisher: John Wiley and Sons
Year: 2007
Tongue: English
Weight: 223 KB
Volume: 96
Category: Article
ISSN: 0006-3592
DOI: 10.1002/bit.21173

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✦ Synopsis

Abstract

A microbial array chip with collagen gel spots entrapping living Escherichia coli (E. coli) DH5α was applied for the screening of recombinant protein solubilities. The α‐fragment of β‐galactosidase (βGal) 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 βGal. 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 βGal activity and therefore, with the soluble fraction of MBP in the host cells. Biotechnol. Bioeng. 2007;96:1008–1013. © 2006 Wiley Periodicals, Inc.

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