Degradation of feather waste by Aspergillus niger keratinases: Comparison of submerged and solid-state fermentation

By A. M. Mazotto, S. Couri, M. Damaso, Alane Beatriz Vermelho. 2013

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Abstract The isolation of native and/or the production of genetically modified enzyme-producing microorganisms may have substantial impacts on industrial processes. In this work twenty-eight Aspergillus niger mutants were screened for peptidases and keratinases production on a basal medium containing chicken feathers (1%). Four strains were selected after preliminary assays: 3T5B8, 9D40, 9D80, and 11D40. The keratinase production was higher when the A. niger strains were cultivated in a solid-state condition rather than a submerged condition: the keratinolytic activity of 3T5B8 strain was 7 times greater when cultivated by solid-state fermentation (SSF). A. niger 3T5B8 had the highest keratinase activity (172.7 U/ml) after seven days at pH 5.0 from solid-state fermentation, whereas the lowest activity was given by A. niger 9D40 after four days (21.3 U/ml) from submerged fermentation. Zymography of culture supernatant showed multiple bands migrating at 40–130, 14–130, displaying activity towards keratin and gelatin substrates, respectively. This is the first study to report production of high molecular mass peptidases using a feather-degrading Aspergillus. Peptidases from strains 3T5B8, 9D40, 9D80, and 11D40 were inhibited by PMSF, except the approximately 40-kDa peptidase, which was inhibited by phenanthroline, indicating the presence of serine and metallopeptidases. The results therefore suggest that the isolates are promising keratinase producers for biotechnological purposes.

Subfields: Biotechnology, Molecular Biology, Plant Science

View Paper: https://www.semanticscholar.org/paper/19798d64e7ed90b6d278ce4dcc9629862f8c2f86

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