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<p>A novel alkaline-stable protease designated BS2 was purified from a newly isolated bacterium, <i>Bacillus safensis</i> S406, through ammonium sulphate (40–60% saturation) precipitation, Sephadex G-75, Mono Q-Sepharose, and ultrafiltration. The purification achieved a 23.57% yield with a 15.36-fold increase in purity. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) analysis revealed an apparent molecular weight of 16.8&#xa0;kDa. The enzyme was completely inhibited by phenylmethanesulfonyl fluoride (PMSF), which suggested its belonging to the serine protease family. The protease exhibited maximum activity at pH 10.0 and 60 °C during casein hydrolysis, with enhanced thermoactivity and thermostability in the presence of 5 mM Mg<sup>2</sup>⁺. BS2 demonstrated remarkable stability under highly alkaline conditions, making it well suited for detergent formulations, where it effectively removed stains at low wash temperatures. Moreover, the stability of BS2 in non-aqueous media is in high demand for its increasing applications in organic synthesis. Additionally, BS2 showed excellent performance in leather processing, enabling efficient and eco-friendly dehairing of goatskins without damaging the pelts, as confirmed by stereoscopic analysis. Collectively, these properties establish BS2 as a promising candidate for diverse industrial applications, particularly in detergent and leather industries.</p>

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A novel protease from Bacillus safensis: application in detergent formulation and goatskins dehairing

  • 期刊论文

  • 发表日期：

    2026年1月8日

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  • Samiha Mhamdi,
  • Naourez Ktari,
  • Khadija Boukholda,
  • Riadh Ben Salah,
  • Moncef Nasri,
  • Alya Sellami Kamoun

摘要

A novel alkaline-stable protease designated BS2 was purified from a newly isolated bacterium, Bacillus safensis S406, through ammonium sulphate (40–60% saturation) precipitation, Sephadex G-75, Mono Q-Sepharose, and ultrafiltration. The purification achieved a 23.57% yield with a 15.36-fold increase in purity. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) analysis revealed an apparent molecular weight of 16.8 kDa. The enzyme was completely inhibited by phenylmethanesulfonyl fluoride (PMSF), which suggested its belonging to the serine protease family. The protease exhibited maximum activity at pH 10.0 and 60 °C during casein hydrolysis, with enhanced thermoactivity and thermostability in the presence of 5 mM Mg2⁺. BS2 demonstrated remarkable stability under highly alkaline conditions, making it well suited for detergent formulations, where it effectively removed stains at low wash temperatures. Moreover, the stability of BS2 in non-aqueous media is in high demand for its increasing applications in organic synthesis. Additionally, BS2 showed excellent performance in leather processing, enabling efficient and eco-friendly dehairing of goatskins without damaging the pelts, as confirmed by stereoscopic analysis. Collectively, these properties establish BS2 as a promising candidate for diverse industrial applications, particularly in detergent and leather industries.