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<p>Nicotinamidase derived from <i>Flammulina velutipes</i> was successfully adsorb/immobilize on chemically treated Japanese cedar biomass, and its physicochemical and catalytic properties were systematically characterized. Enzyme immobilization via column adsorption of crude extract from mushrooms achieved a loading of 15.8&#xa0;mg of protein per gram of support. X-ray photoelectron spectroscopy validated the presence of nitrogen peaks at 399.9–400.0&#xa0;eV, indicative of amino acid residues, thereby verifying successful enzyme attachment. Scanning electron microscopy revealed increased surface roughness following immobilization, and the specific gravity of the support exceeded 1 (dimensionless), indicating its suitability in solid–liquid biocatalytic systems. The immobilized enzyme exhibited optimal activity at 45&#xa0;°C and retained over 80% of its maximum activity across the 37–50&#xa0;°C range. While, the free enzyme lost activity rapidly, retaining only 30% after four days, the immobilized enzyme maintained more than 80% activity even after one month. These findings demonstrate the effectiveness of immobilizing mushroom-derived enzymes on woody biomass supports and underscore the potential of underutilized forest resources for value-added applications.</p>

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Preparation of adsorbed nicotinamidase using Japanese cedar sawdust and its activity properties

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年12月29日

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  • Ryoya Murata,
  • Sumire Tanabe,
  • Masaki Tsujimoto,
  • Shigeru Miyata,
  • Toshiyuki Miyauchi

摘要

Nicotinamidase derived from Flammulina velutipes was successfully adsorb/immobilize on chemically treated Japanese cedar biomass, and its physicochemical and catalytic properties were systematically characterized. Enzyme immobilization via column adsorption of crude extract from mushrooms achieved a loading of 15.8 mg of protein per gram of support. X-ray photoelectron spectroscopy validated the presence of nitrogen peaks at 399.9–400.0 eV, indicative of amino acid residues, thereby verifying successful enzyme attachment. Scanning electron microscopy revealed increased surface roughness following immobilization, and the specific gravity of the support exceeded 1 (dimensionless), indicating its suitability in solid–liquid biocatalytic systems. The immobilized enzyme exhibited optimal activity at 45 °C and retained over 80% of its maximum activity across the 37–50 °C range. While, the free enzyme lost activity rapidly, retaining only 30% after four days, the immobilized enzyme maintained more than 80% activity even after one month. These findings demonstrate the effectiveness of immobilizing mushroom-derived enzymes on woody biomass supports and underscore the potential of underutilized forest resources for value-added applications.