Increasing the catalytic performance of a whole cell biocatalyst harboring a cytochrome P450cam system by stabilization of an electron transfer component

Tsuyoshi Mouri, Noriho Kamiya, Masahiro Goto

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Catalytic activity of a recombinant Escherichia coli whole cell biocatalyst harboring a cytochrome P450cam monooxygenase system from Pseudomonas putida coupled with enzymatic co-factor regeneration was investigated. About 0.7 μmol camphor was hydroxylated per mg dry cells at 4°C in 50 mM Tris/HCl buffer (pH 7.4) when utilizing a stable putidaredoxin (Pdx) mutant, C73S/C85S-Pdx (Cys73Ser, Cys85Ser double mutant), instead of wild-type Pdx, which was about two-fold improvement in the substrate conversion. Ten-micromole camphor was completely hydroxylated at 20°C in 6 h by 15 mg dry cell weight of whole cell biocatalyst including C73S/C85S-Pdx. Thus, modulation of protein-protein interaction in multicomponent enzymatic catalysis in whole cells is important.

Original languageEnglish
Pages (from-to)1509-1513
Number of pages5
JournalBiotechnology letters
Volume28
Issue number18
DOIs
Publication statusPublished - Sep 1 2006

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Fingerprint Dive into the research topics of 'Increasing the catalytic performance of a whole cell biocatalyst harboring a cytochrome P450cam system by stabilization of an electron transfer component'. Together they form a unique fingerprint.

  • Cite this