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Harnessing fragmented cells as biocatalysts : The critical size for sustaining the integrity of the electron transport chain

Hua, Xia ; Hu, Wei ; Hu, Yating ; Pyo, Sang Hyun LU orcid and Xu, Yong (2026) In AIChE Journal 72(5).
Abstract
Biocatalysis has emerged as a cornerstone of sustainable manufacturing, yet conventional modes are hindered by inherent limitations such as metabolic interference, mass transfer barriers, and instability. This study presented a novel platform using fragmented Gluconobacter oxydans, combining the autonomous cofactor regeneration of whole cells with the superior substrate accessibility of free enzymes. It was observed that subcellular membrane fragments retain dehydrogenase activity and an intact electron transport chain (ETC), with a critical size threshold (37,300–250,000 g centrifugal force) systematically validated for sustaining this function. The fragmented cell system eliminates carbon diversion by decoupling catalysis from central... (More)
Biocatalysis has emerged as a cornerstone of sustainable manufacturing, yet conventional modes are hindered by inherent limitations such as metabolic interference, mass transfer barriers, and instability. This study presented a novel platform using fragmented Gluconobacter oxydans, combining the autonomous cofactor regeneration of whole cells with the superior substrate accessibility of free enzymes. It was observed that subcellular membrane fragments retain dehydrogenase activity and an intact electron transport chain (ETC), with a critical size threshold (37,300–250,000 g centrifugal force) systematically validated for sustaining this function. The fragmented cell system eliminates carbon diversion by decoupling catalysis from central metabolism, achieving near-complete substrate conversion across multiple dehydrogenase substrates. Furthermore, artificial electron transfer experiments confirmed the essential role of ETC coupling in the catalytic mechanism. A fully functional FCM system could serve as a scalable and efficient biocatalytic tool for industrial bioconversion processes. (Less)
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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
AIChE Journal
volume
72
issue
5
pages
14 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:105029588755
ISSN
1547-5905
DOI
10.1002/aic.70281
language
English
LU publication?
yes
id
a895906e-67cb-4b7f-9002-08063ef74d0a
date added to LUP
2026-02-07 11:11:43
date last changed
2026-06-10 09:13:07
@article{a895906e-67cb-4b7f-9002-08063ef74d0a,
  abstract     = {{Biocatalysis has emerged as a cornerstone of sustainable manufacturing, yet conventional modes are hindered by inherent limitations such as metabolic interference, mass transfer barriers, and instability. This study presented a novel platform using fragmented Gluconobacter oxydans, combining the autonomous cofactor regeneration of whole cells with the superior substrate accessibility of free enzymes. It was observed that subcellular membrane fragments retain dehydrogenase activity and an intact electron transport chain (ETC), with a critical size threshold (37,300–250,000 g centrifugal force) systematically validated for sustaining this function. The fragmented cell system eliminates carbon diversion by decoupling catalysis from central metabolism, achieving near-complete substrate conversion across multiple dehydrogenase substrates. Furthermore, artificial electron transfer experiments confirmed the essential role of ETC coupling in the catalytic mechanism. A fully functional FCM system could serve as a scalable and efficient biocatalytic tool for industrial bioconversion processes.}},
  author       = {{Hua, Xia and Hu, Wei and Hu, Yating and Pyo, Sang Hyun and Xu, Yong}},
  issn         = {{1547-5905}},
  language     = {{eng}},
  month        = {{02}},
  number       = {{5}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{AIChE Journal}},
  title        = {{Harnessing fragmented cells as biocatalysts : The critical size for sustaining the integrity of the electron transport chain}},
  url          = {{http://dx.doi.org/10.1002/aic.70281}},
  doi          = {{10.1002/aic.70281}},
  volume       = {{72}},
  year         = {{2026}},
}