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Improvement in organophosphorus hydrolase activity of cell surface-engineered yeast strain using Flo1p anchor system

  • Author(s): Fukuda, Takeshi
  • Tsuchiyama, Kouta
  • Makishima, Hirokazu
  • Takayama, Katsumi
  • Mulchandani, Ashok
  • Kuroda, Kouichi
  • Ueda, Mitsuyoshi
  • Suye, Shin-ichiro
  • et al.
Abstract

Organophosphorus hydrolase (OPH) hydrolyzes organophosphorus esters. We constructed the yeast-displayed OPH using Flo1p anchor system. In this system, the N-terminal region of the protein was fused to Flo1p and the fusion protein was displayed on the cell surface. Hydrolytic reactions with paraoxon were carried out during 24 h of incubation of OPH-displaying cells at 30°C. p-Nitrophenol produced in the reaction mixture was detected by HPLC. The strain with highest activity showed 8-fold greater OPH activity compared with cells engineered using glycosylphosphatidylinositol anchor system, and showed 20-fold greater activity than Escherichia coli using the ice nucleation protein anchor system. These results indicate that Flo1p anchor system is suitable for display of OPH in the cell surface-expression systems.

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