Maximizing the efficiency of multienzyme process by stoichiometry optimization

Pavel Dvorak, Nagendra P. Kurumbang, Jaroslav Bendl, Jan Brezovsky, Zbynek Prokop, Jiri Damborsky

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

Multienzyme processes represent an important area of biocatalysis. Their efficiency can be enhanced by optimization of the stoichiometry of the biocatalysts. Here we present a workflow for maximizing the efficiency of a three-enzyme system catalyzing a five-step chemical conversion. Kinetic models of pathways with wild-type or engineered enzymes were built, and the enzyme stoichiometry of each pathway was optimized. Mathematical modeling and one-pot multienzyme experiments provided detailed insights into pathway dynamics, enabled the selection of a suitable engineered enzyme, and afforded high efficiency while minimizing biocatalyst loadings. Optimizing the stoichiometry in a pathway with an engineered enzyme reduced the total biocatalyst load by an impressive 56 %. Our new workflow represents a broadly applicable strategy for optimizing multienzyme processes.

Original languageEnglish
Pages (from-to)1891-1895
Number of pages5
JournalChemBioChem
Volume15
Issue number13
DOIs
StatePublished - 5 Sep 2014
Externally publishedYes

Keywords

  • biocatalysis
  • biotransformations
  • kinetic modeling
  • multienzyme reaction
  • stoichiometry optimization

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