biostudies-literatureKostopoulou AÖsterreichische ForschungsförderungsgesellschaftHorizon 2020 Framework ProgrammeAustrian Federal Ministry of Labour and Economy (BMAW), the Austrian Federal Ministry of Climate Action, Environment, Energy, Mobility, Innovation and Technology (BMK), the Styrian Business Promotion Agency SFG, the Standortagentur Tirol, the Government of Lower Austria, the Business Agency Vienna and BOKU through the COMET Funding Program managed by the Austrian Research Promotion Agency FFG, the Nationalstiftung FTE and the Christian Doppler Research Associatione70106https://www.ebi.ac.uk/biostudies/studies/S-EPMC11816699biostudies-literatureUnknown18(2)The yeast Komagataella phaffii (syn. Pichia pastoris) is a highly effective and well-established host for the production of recombinant proteins. The redox balance of its secretory pathway, which is multi-organelle dependent, is of high importance for producing secretory proteins. Redox imbalance and oxidative stress can significantly influence protein folding and secretion. Glutathione serves as the main redox buffer of the cell and cellular redox conditions can be assessed through the status of the glutathione redox couple (GSH-GSSG). Previous research often focused on the redox potential of the endoplasmic reticulum (ER), where oxidative protein folding and disulphide bond formation occur. In this study, in vivo measurements of the glutathione redox potential were extended to different Microbial biotechnologyImpact of Oxygen Availability on the Organelle-Specific Redox Potentials and Stress in Recombinant Protein Producing Komagataella phaffii.PMC11816699813979Becher DFerrero-Bordera BRebnegger CMattanovich MGasser BKostopoulou AMaaß SMattanovich DfalseImpact of Oxygen Availability on the Organelle-Specific Redox Potentials and Stress in Recombinant Protein Producing Komagataella phaffii.The yeast Komagataella phaffii (syn. Pichia pastoris) is a highly effective and well-established host for the production of recombinant proteins. The redox balance of its secretory pathway, which is multi-organelle dependent, is of high importance for producing secretory proteins. Redox imbalance and oxidative stress can significantly influence protein folding and secretion. Glutathione serves as the main redox buffer of the cell and cellular redox conditions can be assessed through the status of the glutathione redox couple (GSH-GSSG). Previous research often focused on the redox potential of the endoplasmic reticulum (ER), where oxidative protein folding and disulphide bond formation occur. In this study, in vivo measurements of the glutathione redox potential were extended to different 2025-01-01T00:00:00Z2025 Feb2025-04-18T14:36:14.58Z2025-04-04T23:56:24.144ZS-EPMC118166993993716010.1111/1751-7915.70106