@article{fdi:010066794,
  title = {{N}ovel serine keratinase from {C}aldicoprobacter algeriensis exhibiting outstanding hide dehairing abilities},
  author = {{B}ouacem, {K}. and {B}ouanane-{D}arenfed, {A}. and {J}aouadib, {N}. {Z}. and {J}oseph, {M}anon and {H}acene, {H}. and {O}llivier, {B}ernard and {F}ardeau, {M}arie-{L}aure and {B}ejar, {S}. and {J}aouadi, {B}.},
  editor = {},
  language = {{ENG}},
  abstract = {{T}he current paper reports on the purification of an extracellular thermostable keratinase ({KERCA}) produced from {C}aldicoprobacter algeriensis strain {TH}7{C}1({T}), a thermophilic, anaerobic bacterium isolated from a hydrothermal hot spring in {A}lgeria. {T}he maximum keratinase activity recorded after 24-h of incubation at 50 degrees {C} was 21000 {U}/ml. {T}he enzyme was purified by ammonium sulfate precipitation-dialysis and heat treatment (2 h at 50 degrees {C}) followed by {UNO} {Q}-6 {FPLC} anion exchange chromatography, and submitted to biochemical characterization assays. {M}atrix assisted laser desorption ionization-time of flight mass spectrometry ({MALDI}-{TOF}/{MS}) analysis revealed that the purified enzyme was a monomer with a molecular mass of 33246.10 {D}a. {T}he sequence of the 23 {N}-terminal residues of {KERCA} showed high homology with those of bacterial keratinases. {O}ptimal activity was achieved at p{H} 7 and 50 degrees {C}. {T}he enzyme was completely inhibited by phenylmethanesulfonyl fluoride ({PMSF}) and diiodopropyl fluorophosphates ({DFP}), which suggests that it belongs to the serine keratinase family. {KERCA} displayed higher levels of hydrolysis and catalytic efficiency than keratinase {KERQ}7 from {B}acillus tequilensis strain {Q}7. {T}hese properties make {KERCA} a potential promising and eco-friendly alternative to the conventional chemicals used for the dehairing of goat, sheep, and bovine hides in the leather processing industry.},
  keywords = {{C}aldicoprobacter algeriensis ; {K}eratinase ; {L}eather processing industry ; {ALGERIE}},
  booktitle = {},
  journal = {{I}nternational {J}ournal of {B}iological {M}acromolecules},
  volume = {86},
  numero = {},
  pages = {321--328},
  ISSN = {0141-8130},
  year = {2016},
  DOI = {10.1016/j.ijbiomac.2016.01.074},
  URL = {https://www.documentation.ird.fr/hor/fdi:010066794},
}