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Tailoring industrial enzymes for thermostability and activity evolution by the machine learning-based iCASE strategy

Author

Listed:
  • Nan Zheng

    (Jiangnan University)

  • Yongchao Cai

    (Jiangnan University)

  • Zehua Zhang

    (Jiangnan University)

  • Huimin Zhou

    (Jiangnan University)

  • Yu Deng

    (Jiangnan University)

  • Shuang Du

    (Jiangnan University)

  • Mai Tu

    (Jiangnan University)

  • Wei Fang

    (Jiangnan University)

  • Xiaole Xia

    (Jiangnan University
    Tianjin University of Science and Technology)

Abstract

The pursuit of obtaining enzymes with high activity and stability remains a grail in enzyme evolution due to the stability-activity trade-off. Here, we develop an isothermal compressibility-assisted dynamic squeezing index perturbation engineering (iCASE) strategy to construct hierarchical modular networks for enzymes of varying complexity. Molecular mechanism analysis elucidates that the peak of adaptive evolution is reached through a structural response mechanism among variants. Furthermore, this dynamic response predictive model using structure-based supervised machine learning is established to predict enzyme function and fitness, demonstrating robust performance across different datasets and reliable prediction for epistasis. The universality of the iCASE strategy is validated by four sorts of enzymes with different structures and catalytic types. This machine learning-based iCASE strategy provides guidance for future research on the fitness evolution of enzymes.

Suggested Citation

  • Nan Zheng & Yongchao Cai & Zehua Zhang & Huimin Zhou & Yu Deng & Shuang Du & Mai Tu & Wei Fang & Xiaole Xia, 2025. "Tailoring industrial enzymes for thermostability and activity evolution by the machine learning-based iCASE strategy," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-55944-5
    DOI: 10.1038/s41467-025-55944-5
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    References listed on IDEAS

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    2. Kyle K. Nishikawa & Nicholas Hoppe & Robert Smith & Craig Bingman & Srivatsan Raman, 2021. "Epistasis shapes the fitness landscape of an allosteric specificity switch," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
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