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<p>The sweet potato black rot, caused by <i>Ceratocystis fimbriata</i>, leads to substantial postharvest losses in sweet potatoes. This study focused on isolating, purifying, and characterizing the antifungal proteins from <i>Weizmannia coagulans</i> CGMCC 9951 to develop a biological control agent against <i>C. fimbriata</i>. The crude protein, obtained via ammonium sulfate precipitation, was purified through ammonium sulfate fractionation, Sephadex G-75 gel filtration chromatography, and SP Beads 6FF cation exchange chromatography, yielding a single band. The antifungal activity and stability of the purified protein against <i>C. fimbriata</i>, as well as its ability to prevent disease in sweet potatoes, were evaluated. SDS-PAGE and mass spectrometry identified NJ-62 protein, a solute-binding protein family 5 domain-containing protein with a molecular mass of 62.2&#xa0;kDa. The NJ-62 protein has a MIC of 200&#xa0;µg/mL, remained stable across varying temperatures, freeze-thaw cycles, and protease exposures, while maintaining antifungal activity within a pH range of 7–9. The recombinant NJ-62 protein expressed in <i>Escherichia coli</i> also exhibited effective antifungal properties against <i>C. fimbriata</i>. At 200&#xa0;µg/mL, it strongly suppressed the germination of <i>C. fimbriata</i> spores. Furthermore, the NJ-62 protein also significantly reduced the disease incidence in post-harvest sweet potatoes, with inhibition rates of 49.81% (100&#xa0;µg/mL) and 63.15% (200&#xa0;µg/mL). This research provides new insights for sweet potato postharvest storage, highlighting the promising potential and significant research value of <i>W. coagulans</i> CGMCC 9951 in biological applications.</p>

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The Characterization and Antifungal Efficacy of NJ-62 Protein from Weizmannia coagulans CGMCC 9951 against Ceratocystis fimbriata

  • 期刊论文

  • 发表日期：

    2026年4月28日

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  • Jia Xu,
  • Xiaohan Liu,
  • Xin Li,
  • Ying Wu,
  • Pengyan Li,
  • Shanshan Tie,
  • Pingping Tian,
  • Shaobin Gu

摘要

The sweet potato black rot, caused by Ceratocystis fimbriata, leads to substantial postharvest losses in sweet potatoes. This study focused on isolating, purifying, and characterizing the antifungal proteins from Weizmannia coagulans CGMCC 9951 to develop a biological control agent against C. fimbriata. The crude protein, obtained via ammonium sulfate precipitation, was purified through ammonium sulfate fractionation, Sephadex G-75 gel filtration chromatography, and SP Beads 6FF cation exchange chromatography, yielding a single band. The antifungal activity and stability of the purified protein against C. fimbriata, as well as its ability to prevent disease in sweet potatoes, were evaluated. SDS-PAGE and mass spectrometry identified NJ-62 protein, a solute-binding protein family 5 domain-containing protein with a molecular mass of 62.2 kDa. The NJ-62 protein has a MIC of 200 µg/mL, remained stable across varying temperatures, freeze-thaw cycles, and protease exposures, while maintaining antifungal activity within a pH range of 7–9. The recombinant NJ-62 protein expressed in Escherichia coli also exhibited effective antifungal properties against C. fimbriata. At 200 µg/mL, it strongly suppressed the germination of C. fimbriata spores. Furthermore, the NJ-62 protein also significantly reduced the disease incidence in post-harvest sweet potatoes, with inhibition rates of 49.81% (100 µg/mL) and 63.15% (200 µg/mL). This research provides new insights for sweet potato postharvest storage, highlighting the promising potential and significant research value of W. coagulans CGMCC 9951 in biological applications.