Hide depilation and feather disintegration studies with keratinolytic serine protease from a novel Bacillus subtilis isolate

Appl Microbiol Biotechnol. 2008 Mar;78(4):643-50. doi: 10.1007/s00253-008-1355-z. Epub 2008 Feb 9.

Abstract

Keratinases play an important role in biotechnological applications such as improvement of feather meal, enzymatic dehairing and production of amino acids or peptides from high molecular weight substrates. Bacillus subtilis P13, isolated from Vajreshwari hot spring (45-50 degrees C) near Mumbai, India, produces a neutral serine protease and has an optimum temperature of 65 degrees C. This enzyme preparation was keratinolytic in nature and could disintegrate whole chicken feathers, except for the remnants of shafts. The enzyme preparation also exhibited depilation of goat hides with the recovery of intact animal hair. The enzyme preparation could release peptides from ground feathers and bring about their weight reduction; however, similar action on hair was relatively weak. A single major PMSF-sensitive protease band could be detected upon zymogram analysis, indicating that a single enzyme may be responsible for feather degradation and hide depilation. The importance of these findings in the biotechnological application for feather and leather industries is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacillus subtilis / chemistry
  • Bacillus subtilis / classification
  • Bacillus subtilis / enzymology*
  • Bacillus subtilis / isolation & purification
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • Chickens
  • Enzyme Stability
  • Feathers / metabolism*
  • Goats
  • Hair / metabolism
  • Hot Springs / microbiology
  • Humans
  • Hydrogen-Ion Concentration
  • India
  • Industrial Microbiology*
  • Keratins / metabolism*
  • Protease Inhibitors / pharmacology
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / isolation & purification
  • Serine Endopeptidases / metabolism*
  • Substrate Specificity
  • Temperature

Substances

  • Bacterial Proteins
  • Protease Inhibitors
  • Keratins
  • Serine Endopeptidases