Recombinant human myeloperoxidase from Pichia pastoris: Functional analyses and potential for surface applications
Abstract
Human myeloperoxidase (hMPO) catalyzes the conversion of hydrogen peroxide and chloride into hypochlorous acid and plays a key role in human immunity. While commercial MPO is typically purified from human blood or produced recombinantly in mammalian cells or E. coli, we present novel approach for producing active recombinant hMPO (rhMPO) in Pichia pastoris. To eliminate the need for enzyme coupling, we engineered a chimeric protein by combining glucose oxidase from Penicillium amagasakiense and rhMPO. The two open reading frames were fused by PCR, yielding a bifunctional enzyme capable of generating hypochlorous acid directly from glucose. Additionally, the enzymes were immobilized on silicone model substrates via adsorption from solution to generate surface activity. This yeast-based production system provides a cost-effective and scalable platform for large-scale MPO synthesis, opening the development of novel biocatalytic applications.
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BibTeX
@article{ymbe2026recombinant,
title = {{Recombinant human myeloperoxidase from Pichia pastoris: Functional analyses and potential for surface applications}},
author = {Parfait Kenfack Ymbe and Victoria Lublin and Aenora Letourneur and Morrigane Michel and Sébastien Gounel and Gilles Pécastaings and Claire Céré and Valentin Amalric and Nicolas Mousnier and Joanna Giermanska and Jean-Paul Chapel and Claire Stines-Chaumeil},
journal = {Enzyme and Microbial Technology},
year = {2026},
month = aug,
doi = {10.1016/j.enzmictec.2026.110923},
url = {https://hal.science/hal-05732464v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Recombinant human myeloperoxidase from Pichia pastoris: Functional analyses and potential for surface applications
AU - Parfait Kenfack Ymbe
AU - Victoria Lublin
AU - Aenora Letourneur
AU - Morrigane Michel
AU - Sébastien Gounel
AU - Gilles Pécastaings
AU - Claire Céré
AU - Valentin Amalric
AU - Nicolas Mousnier
AU - Joanna Giermanska
AU - Jean-Paul Chapel
AU - Claire Stines-Chaumeil
PY - 2026
DA - 2026/08/31
JO - Enzyme and Microbial Technology
DO - 10.1016/j.enzmictec.2026.110923
UR - https://hal.science/hal-05732464v1
AB - Human myeloperoxidase (hMPO) catalyzes the conversion of hydrogen peroxide and chloride into hypochlorous acid and plays a key role in human immunity. While commercial MPO is typically purified from human blood or produced recombinantly in mammalian cells or E. coli, we present novel approach for producing active recombinant hMPO (rhMPO) in Pichia pastoris. To eliminate the need for enzyme coupling, we engineered a chimeric protein by combining glucose oxidase from Penicillium amagasakiense and rhMPO. The two open reading frames were fused by PCR, yielding a bifunctional enzyme capable of generating hypochlorous acid directly from glucose. Additionally, the enzymes were immobilized on silicone model substrates via adsorption from solution to generate surface activity. This yeast-based production system provides a cost-effective and scalable platform for large-scale MPO synthesis, opening the development of novel biocatalytic applications.
SN - 0141-0229
ER -