Biodegradation of Feather Waste Keratin by the Keratin-Degrading Strain Bacillus subtilis 8

J Microbiol Biotechnol. 2018 Feb 28;28(2):314-322. doi: 10.4014/jmb.1708.08077.

Abstract

Bacillus subtilis 8 is highly efficient at degrading feather keratin. We observed integrated feather degradation over the course of 48 h in basic culture medium while studying the entire process with scanning electron microscopy. Large amounts of ammonia, sulfite, and L-cysteic acid were detected in the fermented liquid. In addition, four enzymes (gamma-glutamyltranspeptidase, peptidase T, serine protease, and cystathionine gamma-synthase) were identified that play an important role in this degradation pathway, all of which were verified with molecular cloning and prokaryotic expression. To the best of our knowledge, this report is the first to demonstrate that cystathionine gamma-synthase secreted by B. subtilis 8 is involved in the decomposition of feather keratin. This study provides new data characterizing the molecular mechanism of feather degradation by bacteria, as well as potential guidance for future industrial utilization of waste keratin.

Keywords: Bacillus subtilis; degradation mechanism; keratin; prokaryotic expression; purification.

MeSH terms

  • Amino Acids / analysis
  • Ammonia / metabolism
  • Animals
  • Bacillus subtilis / enzymology
  • Bacillus subtilis / genetics
  • Bacillus subtilis / metabolism*
  • Biodegradation, Environmental
  • Chickens
  • Cloning, Molecular
  • Culture Media / chemistry
  • Cysteic Acid / metabolism
  • Feathers / metabolism*
  • Fermentation*
  • Gene Expression Regulation, Bacterial
  • Industrial Microbiology
  • Keratins / metabolism*
  • Microscopy, Electron, Scanning
  • Peptide Hydrolases / isolation & purification
  • Peptide Hydrolases / metabolism*
  • Sulfites / analysis
  • Sulfites / metabolism

Substances

  • Amino Acids
  • Culture Media
  • Sulfites
  • Keratins
  • Ammonia
  • Cysteic Acid
  • Peptide Hydrolases
  • keratinase