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Hydrolyzing Proficiency of Keratinases in Feather Degradation

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Abstract

The keratinase degrade highly rigid, cross linked structural polypeptides with different efficiency depending on the type of source. Two newly isolated strains of Bacillus subtilis (RSE163 and RSE165; NCBI Accession no JQ887983 and JQ887982) were found to be efficient keratinase producers with unusual catalytic activity result in different morphological changes in degradation pattern of feather, confirmed by their scanned electron micrographs. Maximum keratinolytic activity of both the strains B. subtilis RSE163 and RSE165 were found to be 366 ± 15.79 and 194 ± 7.26 U after 72 h of incubation. While the disulphide reductase activity of RSE163 and RSE165 estimated 0.24 ± 0.05 and 0.15 ± 0.03 U/ml of enzyme after 24 h of incubation. A total of 16 free amino acids of variable concentration were also analyzed in the cell free supernatant of hydrolyzed feather from two strains. Present study demonstrates the action of two different keratinases in feather degradation.

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Acknowledgments

We acknowledge Department of Anatomy, AIIMS, New Delhi, for helping the SEM analysis facility. We also extend our sincere thanks to Ministry of Environment for providing the funds and senior research fellowship to Ms Sonali Gupta.

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  1. Amity Institute of Microbial Biotechnology, Amity University, Sector-125, Noida, Uttar Pradesh, India

    Sonali Gupta & Rajni Singh

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  1. Sonali Gupta
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  2. Rajni Singh
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Correspondence to Rajni Singh.

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Gupta, S., Singh, R. Hydrolyzing Proficiency of Keratinases in Feather Degradation. Indian J Microbiol 54, 466–470 (2014). https://doi.org/10.1007/s12088-014-0477-5

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  • DOI: https://doi.org/10.1007/s12088-014-0477-5

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