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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
  • Georgia Institute of Technology

Research output: Contribution to journal › Journal article › Research › peer-review

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Abstract

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
Volume297
Number of pages13
ISSN0009-2509
DOIs
Publication statusPublished - 2024

Keywords

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

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