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<p>This study quantified the production, purification, enzymatic characteristics, and xylan film modification performance of extracellular xylanase (XynA) from <i>Thermomyces dupontii</i> J22. The thermostable xylanase activity attained 768.32 U/mL in the fermentation broth via submerged fermentation using corn cob as the substrate. XynA was purified to electrophoretic homogeneity by ammonium sulfate precipitation and DEAE-Cellulose chromatography, achieving a final specific activity of 59019.65 U/mg, a 26.18-fold purification, and a recovery yield of 40.52%. The molecular weight of XynA was approximately 24&#xa0;kDa. XynA displayed an optimal pH of 7.5 and optimal temperature of 75 ℃, and was rapidly thermally activated at 55–60 ℃ while retaining high activity under alkaline conditions. The <i>K</i><sub><i>m</i></sub> values for beechwood and wheat xylan were 2.50 and 3.21&#xa0;mg/mL, respectively, with corresponding <i>V</i><sub><i>max</i></sub> values of 138.90 and 111.30 µmol·min<sup>− 1</sup>. XynA activity was enhanced by Na<sup>+</sup>, K<sup>+</sup>, Mg<sup>2+</sup>, Triton X-100, and β-mercaptoethanol. In xylan film modification, XynA treatment reduced tensile strength by only 16.88%, compared to a 56.25% reduction with NaOH treatment, while preserving a Young’s modulus of 4.05 GPa. Atomic force microscopy and X-ray diffraction showed that XynA generated a uniform grid microstructure on film surfaces without severe structural damage. These results demonstrate that XynA is a highly efficient thermostable xylanase suitable for mild, eco-friendly functional modification of xylan-based biomaterials.</p>

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A highly efficient thermostable xylanase from Thermomyces dupontii J22: purification, properties and its application in xylan film modification

  • 期刊论文

  • 发表日期：

    2026年7月20日

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  • Weiwei Fu,
  • Qiang Li,
  • Chao Teng,
  • Qijie Sun,
  • Chunyan Huo,
  • Ning Cai,
  • Guangsen Fan,
  • Yunping Zhu

摘要

This study quantified the production, purification, enzymatic characteristics, and xylan film modification performance of extracellular xylanase (XynA) from Thermomyces dupontii J22. The thermostable xylanase activity attained 768.32 U/mL in the fermentation broth via submerged fermentation using corn cob as the substrate. XynA was purified to electrophoretic homogeneity by ammonium sulfate precipitation and DEAE-Cellulose chromatography, achieving a final specific activity of 59019.65 U/mg, a 26.18-fold purification, and a recovery yield of 40.52%. The molecular weight of XynA was approximately 24 kDa. XynA displayed an optimal pH of 7.5 and optimal temperature of 75 ℃, and was rapidly thermally activated at 55–60 ℃ while retaining high activity under alkaline conditions. The Km values for beechwood and wheat xylan were 2.50 and 3.21 mg/mL, respectively, with corresponding Vmax values of 138.90 and 111.30 µmol·min− 1. XynA activity was enhanced by Na+, K+, Mg2+, Triton X-100, and β-mercaptoethanol. In xylan film modification, XynA treatment reduced tensile strength by only 16.88%, compared to a 56.25% reduction with NaOH treatment, while preserving a Young’s modulus of 4.05 GPa. Atomic force microscopy and X-ray diffraction showed that XynA generated a uniform grid microstructure on film surfaces without severe structural damage. These results demonstrate that XynA is a highly efficient thermostable xylanase suitable for mild, eco-friendly functional modification of xylan-based biomaterials.