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Microbial keratinases provide an eco-friendly alternative approach for bioconversion of poultry wastes. The present study was designed with an objective to purify and characterize the keratinase enzyme from preidentified Bacillus subtilis strain AJ. The keratinase secreted by bacteria have molecular weight ~64 kDa. The chicken feathers were used as a source of carbon and nitrogen in the medium. Two successive steps were employed for purification of the keratinase enzyme- ion exchange chromatography on CM-cellulose followed by gel filtration on sephadex G-50 column. The enzyme showed a specific activity of 820 U mg−1 against 91.24 U mg−1 proteins for crude extract with 9 fold purification. At optimum pH 9.0 and temperature 40 °C purified enzyme showed maximum activity when keratin powder was used as a substrate. The enzyme was maximally active in the presence of Zn+2 ions as compared to other metal ions such as Ni+2, Cu+2, Hg+2 and Co+2. The presence of SDS enhances the enzyme activity whereas the EDTA, DMSO, methanol and ethanol reduce its activity. In conclusion: Bacillus subtilis strain AJ demonstrated the potential to degrade feather waste with the production of keratinase.

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Partial Purification and Characterization of Keratinase from Feather Degrading Bacillus subtilis Strain AJ

  • 会议论文

  • 发表日期：

    2025年

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  • Sunil Chhimpa,
  • Manish Soni,
  • Chandra Shekhar Yadav,
  • Kanti Prakash Sharma,
  • Kumud Kant Awasthi,
  • P. J. John

摘要

Microbial keratinases provide an eco-friendly alternative approach for bioconversion of poultry wastes. The present study was designed with an objective to purify and characterize the keratinase enzyme from preidentified Bacillus subtilis strain AJ. The keratinase secreted by bacteria have molecular weight ~64 kDa. The chicken feathers were used as a source of carbon and nitrogen in the medium. Two successive steps were employed for purification of the keratinase enzyme- ion exchange chromatography on CM-cellulose followed by gel filtration on sephadex G-50 column. The enzyme showed a specific activity of 820 U mg−1 against 91.24 U mg−1 proteins for crude extract with 9 fold purification. At optimum pH 9.0 and temperature 40 °C purified enzyme showed maximum activity when keratin powder was used as a substrate. The enzyme was maximally active in the presence of Zn+2 ions as compared to other metal ions such as Ni+2, Cu+2, Hg+2 and Co+2. The presence of SDS enhances the enzyme activity whereas the EDTA, DMSO, methanol and ethanol reduce its activity. In conclusion: Bacillus subtilis strain AJ demonstrated the potential to degrade feather waste with the production of keratinase.