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<p>Catalase plays a significant role in improving animal intestinal health and growth performance; however, its industrial application in feed is largely limited by poor thermostability and low acid tolerance. We identified an acid-resistant catalase from <i>Talaromyces pinophilus</i> and improved its thermal stability. We integrated multiple thermal stability design strategies, constructed a mutation library using algorithms from different design platforms, and further refined the library with computational tools. This approach successfully generated the combinatorial mutant M3 (E38Q/S69P/S187A). Its half-life at 80&#xa0;°C increased by 2.64 times, and two fold increase in half life at 90 ℃, while the specific activity remained unchanged. Molecular dynamics simulations show that this mutational strategy can significantly enhance the thermal stability of catalase through a cascading effect of ‘local rigidity enhancement—global conformational compaction—hydrophobic core stabilization’. Additionally, under simulated high-temperature and gastric acid conditions, the mutant strain demonstrated a high capacity for decomposing H<sub>2</sub>O<sub>2</sub>, significantly enhancing its practical value for use in animal feed.</p> Graphical abstract <p></p>

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Thermostability modification and simulated application of acidic catalase

  • 期刊论文

  • 发表日期：

    2026年8月3日

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  • Yuxue Duan,
  • Xiaowei Yu,
  • Pu Zheng,
  • Pengcheng Chen,
  • Dan Wu

摘要

Catalase plays a significant role in improving animal intestinal health and growth performance; however, its industrial application in feed is largely limited by poor thermostability and low acid tolerance. We identified an acid-resistant catalase from Talaromyces pinophilus and improved its thermal stability. We integrated multiple thermal stability design strategies, constructed a mutation library using algorithms from different design platforms, and further refined the library with computational tools. This approach successfully generated the combinatorial mutant M3 (E38Q/S69P/S187A). Its half-life at 80 °C increased by 2.64 times, and two fold increase in half life at 90 ℃, while the specific activity remained unchanged. Molecular dynamics simulations show that this mutational strategy can significantly enhance the thermal stability of catalase through a cascading effect of ‘local rigidity enhancement—global conformational compaction—hydrophobic core stabilization’. Additionally, under simulated high-temperature and gastric acid conditions, the mutant strain demonstrated a high capacity for decomposing H2O2, significantly enhancing its practical value for use in animal feed.

Graphical abstract