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Abstract <p>To mitigate the increase in <i>Staphylococcus aureus</i> resistance resulting from antibiotic misuse, this study aimed to identify natural and safe antibacterial substances as alternatives to conventional antibiotics for treating <i>S. aureus</i> infections in animal husbandry. An antibacterial protein (APBS) with broad pH and thermal stability was successfully purified from the culture supernatant of <i>Bacillus subtilis</i> FB123 using ammonium sulfate precipitation, Sephacryl S-200 High Resolution gel filtration chromatography, and DEAE Sepharose Fast Flow ion exchange chromatography. APBS exhibited a significant inhibitory effect against <i>S.&#xa0;aureus,</i> producing an inhibition zone diameter up to 16.5 mm. Investigation of its physicochemical properties revealed that APBS displayed optimal antibacterial activity at 30°C and pH 6.0, and retained high activity even after treatment at 121°C and across a broad pH range from 2.0 to 9.0. The molecular weight of APBS was estimated to be approximately 14.8 kDa by SDS-PAGE, and its isoelectric point was determined to be 3.64. Furthermore, this protein demonstrated broad spectrum of antibacterial activity against other Gram-positive bacteria and fungi. Finally, the effects of various proteases, metal ions, and organic solvents on its activity were investigated to assess the potential practical application of APBS. This study indicates that the APBS from <i>B. subtilis</i> FB123 holds promising potential for development as a novel anti-<i>S. aureus</i> agent.</p>

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Biochemical Characterization of a Thermostable Broad-pH Antimicrobial Protein from Bacillus subtilis FB123

  • 期刊论文

  • 发表日期：

    2026年7月9日

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  • X. Luo,
  • Y. Lin,
  • B. Shi

摘要

Abstract

To mitigate the increase in Staphylococcus aureus resistance resulting from antibiotic misuse, this study aimed to identify natural and safe antibacterial substances as alternatives to conventional antibiotics for treating S. aureus infections in animal husbandry. An antibacterial protein (APBS) with broad pH and thermal stability was successfully purified from the culture supernatant of Bacillus subtilis FB123 using ammonium sulfate precipitation, Sephacryl S-200 High Resolution gel filtration chromatography, and DEAE Sepharose Fast Flow ion exchange chromatography. APBS exhibited a significant inhibitory effect against S. aureus, producing an inhibition zone diameter up to 16.5 mm. Investigation of its physicochemical properties revealed that APBS displayed optimal antibacterial activity at 30°C and pH 6.0, and retained high activity even after treatment at 121°C and across a broad pH range from 2.0 to 9.0. The molecular weight of APBS was estimated to be approximately 14.8 kDa by SDS-PAGE, and its isoelectric point was determined to be 3.64. Furthermore, this protein demonstrated broad spectrum of antibacterial activity against other Gram-positive bacteria and fungi. Finally, the effects of various proteases, metal ions, and organic solvents on its activity were investigated to assess the potential practical application of APBS. This study indicates that the APBS from B. subtilis FB123 holds promising potential for development as a novel anti-S. aureus agent.