@article{fdi:010074935,
  title = {{P}urification and biochemical characterization of a novel acido-halotolerant and thermostable endochitinase from {M}elghiribacillus thermohalophilus strain {N}ari2{A}({T})},
  author = {{M}ohamed, {S}. and {B}ouacem, {K}. and {M}echri, {S}. and {A}ddou, {N}. {A}. and {L}aribi-{H}abchi, {H}. and {F}ardeau, {M}arie-{L}aure and {J}aouadi, {B}. and {B}ouanane-{D}arenfed, {A}. and {H}acene, {H}.},
  editor = {},
  language = {{ENG}},
  abstract = {{A}n extracellular acido-thermostable endochitinase (called {C}hi{A}-{M}t45) from thermohalophilic {M}elghiribacillus thermohalophilus strain {N}ari2{A}({T}) gen. nov. sp. nov., was purified and biochemically characterized. {T}he maximum chitinase activity recorded after 48-h of incubation at 55 degrees {C} was 9000 {U}/m{L}. {P}ure enzyme was obtained after heat treatment (20 min at 90 degrees {C}) followed by sequential column chromatographies on fast performance liquid chromatography ({FPLC}) and high performance liquid chromatography ({HPLC}). {B}ased on {MALDI}-{TOF}/{MS} analysis, the purified enzyme is a monomer with a molecular mass of 45201.10 {D}a. {T}he 27 residue {NH}2-terminal sequence of the enzyme showed high homology with {B}acillus {GH}-18 chitinases family. {T}he optimum p{H} and temperature values for chitinase activity were p{H} 3.5 and 90 degrees {C}, respectively. {I}n addition, the enzyme was halotolerant and can be classified as an extremozyme. {T}he pure enzyme was completely inhibited by p-chloromercuribenzoic acid (p-{CMB}) and {N}-ethylmaleimide ({NEM}). {I}ts {K}-m and k(cat) values were 0.253 mg colloidal chitin/m{L} and 47000 s(-1), respectively. {I}nterestingly, its catalytic efficiency was higher than those of chitinases {C}hi{A}-{H}h59 from {H}ydrogenophilus hirchii {KB}-{DZ}44 and chitodextrinase from {S}treptomyces griseus, and {N}-acetyl-beta-glucosaminidase from {T}richoderma viride. {T}he studied chitinase exhibited high activity towards colloidal chitin, chitin azure, glycol chitin, while it did not hydrolyse chitibiose and amylose. {A}dditionally, thin-layer chromatography ({TLC}) analysis from chitin-oligosaccharides showed that {C}hi{A}-{M}t45 acted as an endosplitting enzyme. {O}verall, the chitinase {C}hi{A}-{M}t45 may have great potential for the enzymatic degradation of chitin.},
  keywords = {{C}hitinase ; {C}hitin ; {M}elghiribacillus thermohalophilus ; {T}hin-layer chromatography ; {H}ydrolytic pattern ; {ALGERIE} ; {SAHARA}},
  booktitle = {},
  journal = {{C}arbohydrate {R}esearch},
  volume = {473},
  numero = {},
  pages = {46--56},
  ISSN = {0008-6215},
  year = {2019},
  DOI = {10.1016/j.carres.2018.12.017},
  URL = {https://www.documentation.ird.fr/hor/fdi:010074935},
}