Isolation and characterization of a feather-degrading enzyme from Bacillus pseudofirmus FA30-01

Extremophiles. 2006 Jun;10(3):229-35. doi: 10.1007/s00792-005-0491-y. Epub 2006 Feb 18.

Abstract

We isolated the feather-degrading Bacillus pseudofirmus FA30-01 from the soil sample of poultry farm. The isolate completely degraded feather pieces after liquid culture at 30 degrees C (pH 10.5) for 3 days. Strain FA30-01 is a Gram-positive, spore-forming, rod-shaped bacterium and was identified with B. pseudofirmus based on 16S rDNA analysis. The keratinase enzyme produced by strain FA30-01 was refined using ammonium sulfate precipitation, negative-ion DEAE Toyopearl exchange chromatography, and hydroxyapatite chromatography. The refinement level was 14.5-fold. The molecular weight of this enzyme was 27.5 kDa and it had an isoelectric point of 5.9. The enzyme exhibited activity at pH 5.1-11.5 and 30-80 degrees C with azokeratin as a substrate, although the optimum pH and temperature for keratinase activity were pH 8.8-10.3 and 60 degrees C, respectively. This enzyme is one of the serine-type proteases. Subtilisin ALP I and this enzyme had 90% homology in the N-terminal amino acid sequence. Since this enzyme differed from ALP I in molecular weight, heat resistance and isoelectric point, they are suggested to be different enzymes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacillus / classification*
  • Bacillus / drug effects
  • Bacillus / enzymology*
  • Culture Media
  • Feathers / metabolism*
  • Hydrogen-Ion Concentration
  • Molecular Sequence Data
  • Peptide Hydrolases / chemistry
  • Peptide Hydrolases / isolation & purification*
  • Peptide Hydrolases / metabolism*
  • Protease Inhibitors / pharmacology
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Temperature

Substances

  • Culture Media
  • Protease Inhibitors
  • Peptide Hydrolases
  • keratinase