@article{fdi:010066066,
  title = {{B}iochemical characterization of a detergent-stable serine alkaline protease from {C}aldicoprobacter guelmensis},
  author = {{B}ouacem, {K}. and {B}ouanane-{D}arenfed, {A}. and {L}aribi-{H}abchi, {H}. and {B}en {E}lhoul, {M}. and {H}mida-{S}ayari, {A}. and {H}acene, {H}. and {O}llivier, {B}ernard and {F}ardeau, {M}arie-{L}aure and {J}aouadi, {B}. and {B}ejar, {S}.},
  editor = {},
  language = {{ENG}},
  abstract = {{C}aldicoprobacter guelmensis isolated from the hydrothermal hot spring of {G}uelma ({A}lgeria) produced high amounts of extracellular thermostable serine alkaline protease (called {SAPCG}) (23,000 {U}/m{L}). {T}he latter was purified by ammonium sulphate precipitation, {UNO} {Q}-6 {FPLC} and {Z}orbex {PSM} 300 {HPLC}, 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 55,824.19 {D}a. {T}he 19 {N}-terminal residue sequence of {SAPCG} showed high homology with those of microbial proteases. {T}he enzyme was completely inhibited by phenylmethanesulfonyl fluoride ({PMSF}) and diiodopropyl fluorophosphates ({DFP}), which suggested its belonging to the serine protease family. {I}t showed optimum protease activity at p{H} 10 and 70 degrees {C} with casein as a substrate. {T}he thermoactivity and thermostability of {SAPCG} were enhanced in the presence of 2 m{M} {C}a2+. {I}ts half-life times at 80 and 90 degrees {C} were 180 and 60 min, respectively. {I}nterestingly, the {SAPCG} protease exhibited significant compatibility with i{S}i{S} and {P}ersil, and wash performance analysis revealed that it could remove bloodstains effectively. {O}verall, {SAPCG} displayed a number of attractive properties that make it a promising candidate for future applications as an additive in detergent formulations.},
  keywords = {{P}rotease ; {C}aldicoprobacter guelmensis ; {D}etergent formulations ; {ALGERIE}},
  booktitle = {},
  journal = {{I}nternational {J}ournal of {B}iological {M}acromolecules},
  volume = {81},
  numero = {},
  pages = {299--307},
  ISSN = {0141-8130},
  year = {2015},
  DOI = {10.1016/j.ijbiomac.2015.08.011},
  URL = {https://www.documentation.ird.fr/hor/fdi:010066066},
}