ArticleArchives of microbiology2025
High-level expression of zearalenone lactonohydrolase ZenG in Pichia pastoris via combinatorial strategy.
Article in Archives of microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Zearalenone contamination poses a continuing threat to food security and the health of the livestock industry; developing efficient, high-yield detoxifying enzyme formulations is therefore essential. This study aimed to achieve the high-level expression of zearalenone lactonohydrolase ZenG in Pichia pastoris. The resulting recombinant ZenG exhibited optimal activity at pH 8.0 and 50 °C, with a specific activity of 684 ± 2.17 U/mg. Replacing the α-factor signal peptide with the pre-Ost1-pro-α-factor signal peptide increased ZenG activity from 180.26 U/mL to 276.47 U/mL. Subsequent optimization of the gene dosage further boosted the yield to 479.52 U/mL. Co-expression of the molecular chaperones 100p-HAC and 55p-HAC1 elevated the enzyme activity to 557.85 U/mL and 582.01 U/mL, which correspond to 3.09-fold and 3.23-fold increases, respectively, compared to the initial G-α-ZenG strain. In conclusion, this study successfully constructed an engineered P. pastoris strain capable of highly efficient ZenG production, laying a solid foundation for its industrial-scale application.
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