Scholarlink

<p>Microbial keratin degradation has been recognized as a sustainable strategy for treating keratin-rich residues, as it avoids the use of environmentally harmful chemical agents. The present study aimed to evaluate the ability of <i>Bacillus subtilis</i> to degrade chicken feathers and to characterize the proteolytic enzymes it secretes. The enzymes were produced by <i>B. subtilis</i> in submerged fermentation, using chicken feathers (0.5% w/v) as the sole source of carbon and nitrogen. The resulting enzymatic extract contained multiple proteases, as evidenced by their detection in polyacrylamide gels copolymerized with gelatin. This extract exhibited distinct optimal pH ranges for keratinolytic and caseinolytic activities. Inhibition assays revealed that keratinolytic activity was strongly affected by phenylmethylsulfonyl fluoride (PMSF), with reductions of 49.3% at pH 7.0 and 88.4% at pH 9.5, and by ethylenediaminetetraacetic acid (EDTA), which caused inhibitions of 69.2% and 78.7% at pH 7.0 and 9.5, respectively. Caseinolytic activity was even more sensitive to these inhibitors, particularly at pH 9.5. Enzymes exhibiting higher activity at pH 7.0 displayed a greater capacity to hydrolyze native keratinous substrates compared with those active under alkaline conditions. Overall, these findings highlight <i>B. subtilis</i> as a promising source of keratinolytic enzymes with favorable biochemical properties for biotechnological applications, including biofilm dispersion and production of bioactive peptides.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Keratinolytic proteases secreted by Bacillus subtilis obtained from feather-based submerged culture

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年6月18日

查看全文
  • Cíntia Lionela Ambrósio de Menezes,
  • Rafael Amadeu Barreto,
  • Emanuella Roberto Ribeiro,
  • Érike Jhonnathan Pereira,
  • Luana De Lucca Thomaz,
  • Maurício Boscolo,
  • Roberto da Silva,
  • Eleni Gomes,
  • Ronivaldo Rodrigues da Silva

摘要

Microbial keratin degradation has been recognized as a sustainable strategy for treating keratin-rich residues, as it avoids the use of environmentally harmful chemical agents. The present study aimed to evaluate the ability of Bacillus subtilis to degrade chicken feathers and to characterize the proteolytic enzymes it secretes. The enzymes were produced by B. subtilis in submerged fermentation, using chicken feathers (0.5% w/v) as the sole source of carbon and nitrogen. The resulting enzymatic extract contained multiple proteases, as evidenced by their detection in polyacrylamide gels copolymerized with gelatin. This extract exhibited distinct optimal pH ranges for keratinolytic and caseinolytic activities. Inhibition assays revealed that keratinolytic activity was strongly affected by phenylmethylsulfonyl fluoride (PMSF), with reductions of 49.3% at pH 7.0 and 88.4% at pH 9.5, and by ethylenediaminetetraacetic acid (EDTA), which caused inhibitions of 69.2% and 78.7% at pH 7.0 and 9.5, respectively. Caseinolytic activity was even more sensitive to these inhibitors, particularly at pH 9.5. Enzymes exhibiting higher activity at pH 7.0 displayed a greater capacity to hydrolyze native keratinous substrates compared with those active under alkaline conditions. Overall, these findings highlight B. subtilis as a promising source of keratinolytic enzymes with favorable biochemical properties for biotechnological applications, including biofilm dispersion and production of bioactive peptides.