Towards a mechanistic model of oxidase deactivation in a bubble column

Amalie Vang Høst, John M. Woodley*, Andreas S. Bommarius

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review


Despite the many advantages of biocatalysis, enzyme stability remains an issue. This work investigates the long-term kinetic stability of a water-forming NAD(P)H-oxidase (NOX2), an enzyme of potential industrial interest for NAD(P)H regeneration, in a bubble column sparged with air, which enables reasonable oxygen transfer but without drastic enzyme deactivation. Experiments have been performed with the particular goal of explaining the observed two-stage deactivation trend. We show evidence supporting the hypothesis that the first stage is related to the adsorption of enzymes to the interface, followed by a subsequent deactivation stage at the interface.

The characterization of NOX deactivation in the bubble column setup, complemented by additional’quiescent’ experiments, has enabled the development of a first principles model as the first step towards a complete mechanistic model of oxidase deactivation at gas–liquid interfaces.
Original languageEnglish
Article number120282
JournalChemical Engineering Science
Number of pages13
Publication statusPublished - 2024


  • Bubble column
  • Gas-liquid interface
  • Kinetic stability
  • Oxidases
  • Two-stage deactivation trend


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