Expression levels of chaperones influence biotransformation activity of recombinant Escherichia coli expressing Micrococcus luteus alcohol dehydrogenase and Pseudomonas putida Baeyer-Villiger monooxygenase

A. Hyong Baek, Eun Yeong Jeon, Sun Mee Lee, Jin Byung Park

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

We demonstrated for the first time that the archaeal chaperones (i.e., γ-prefoldin and thermosome) can stabilize enzyme activity in vivo. Ricinoleic acid biotransformation activity of recombinant Escherichia coli expressing Micrococcus luteus alcohol dehydrogenase and the Pseudomonas putida KT2440 Baeyer-Villiger monooxygenase improved significantly with co-expression of γ-prefoldin or recombinant themosome originating from the deep-sea hyperthermophile archaea Methanocaldococcus jannaschii. Furthermore, the degree of enhanced activity was dependent on the expression levels of the chaperones. For example, whole-cell biotransformation activity was highest at 12μmol/g dry cells/min when γ-prefoldin expression level was approximately 46% of the theoretical maximum. This value was approximately two-fold greater than that in E. coli, where the γ-prefoldin expression level was zero or set to the theoretical maximum. Therefore, it was assumed that the expression levels of chaperones must be optimized to achieve maximum biotransformation activity in whole-cell biocatalysts.

Original languageEnglish
Pages (from-to)889-895
Number of pages7
JournalBiotechnology and Bioengineering
Volume112
Issue number5
DOIs
StatePublished - 1 May 2015

Keywords

  • Alcohol dehydrogenase
  • Baeyer-Villiger monooxygenase
  • Chaperones
  • Escherichia coli
  • Ricinoleic acid
  • Thermosome
  • Whole-cell biocatalysis
  • γ-prefoldin

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