Trehalose metabolism plays a crucial role in yeast stress tolerance during biomass propagation and dehydration, but its regulatory mechanisms under these industrial conditions remain incompletely understood. This study analyses the role of an antioxidant enzyme, the cytosolic peroxiredoxin Tsa1, in modulating trehalose metabolism in Saccharomyces cerevisiae wine strains during biomass production in molasses. Through comparative analyses in three commercial genetic backgrounds (L2056, T73, EC1118), we demonstrate that TSA1 deletion generally leads to increased intracellular trehalose accumulation despite phenotypic variability among strains. Enzymatic assays revealed that Tsa1 does not regulate trehalose synthesis by altering glycolytic/gluconeogenic flux through pyruvate kinase. However, the deletion of TSA1 resulted in increased oxidation of trehalose synthesis enzymes, as well as enhanced activity of trehalose-6-phosphate synthase and the trehalases Nth1 and Ath1, suggesting the involvement of peroxiredoxin in the futile cycle of trehalose synthesis and degradation. Scaling up the yeast biomass propagation process to semi-industrial conditions confirmed these findings, with increased trehalose levels in the tsa1∆ mutant correlating with enhanced desiccation resistance of the resulting biomass. These results highlight a novel Tsa1-dependent regulatory mechanism governing trehalose metabolism beyond its canonical antioxidant role. Understanding this pathway provides new insights into optimising yeast biomass propagation for industrial applications.
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Evidence ID | Analyze ID | Gene/Complex | Systematic Name/Complex Accession | Qualifier | Gene Ontology Term ID | Gene Ontology Term | Aspect | Annotation Extension | Evidence | Method | Source | Assigned On | Reference |
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Evidence ID | Analyze ID | Dataset | Description | Keywords | Number of Conditions | Reference |
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