title: Production, purification and characterization of an extracellular keratinase from Lysobacter NCIMB 9497.
abstract: OBJECTIVE
  The aim of this study was to determine the keratinolytic ability of a range of bacteria and subsequently, to characterize the keratinase showing the greatest biotechnological potential.
  
  
  RESULTS
  Nine bacteria, reported to produce extracellular proteases, were screened for production of keratinases. Of these, Lysobacter NCIMB 9497 exhibited the highest keratinolytic activity. The keratinase from this strain (Mr 148 kDa) was purified and characterized. Optimum activity occurred at 50 degrees C; no inhibition was demonstrated by phenylmethylsulphonyl fluoride (PMSF), but inhibition by EDTA was demonstrated.
  
  
  CONCLUSIONS
  This study indicates that keratinase is a metalloprotease with a high degree of keratinolytic activity and stability.
  
  
  CONCLUSIONS
  This is the first detailed report of a metalloprotease with keratinolytic activity. The novel reaction mechanism, degree of keratinolytic activity and stability indicate considerable biotechnological potential in the leather industry, and in the processing of poultry waste.
authors.affiliation: Department of Biological Sciences, Staffordshire University, Stoke-on-Trent, UK.
authors.forename: J D
authors.initials: JD
authors.lastname: Allpress
authors.forename: G
authors.initials: G
authors.lastname: Mountain
authors.forename: P C
authors.initials: PC
authors.lastname: Gowland
mesh_terms: D002364:Caseins / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D007633:Keratins / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000096:biosynthesis* / Q000302:isolation & purification
chemical_list: D002364:Caseins; D007633:Keratins; D010447:Peptide Hydrolases; C035855:keratinase