@article{fdi:010066074,
  title = {{C}haracterization of a purified thermostable xylanase from {C}aldicoprobacter algeriensis sp. nov. strain {TH}7{C}1({T})},
  author = {{B}ouanane-{D}arenfed, {A}. and {B}oucherba, {N}. and {B}ouacem, {K}. and {G}agaoua, {M}. and {J}oseph, {M}. and {K}ebbouche-{G}ana, {S}. and {N}ateche, {F}. and {H}acene, {H}. and {O}llivier, {B}ernard and {C}ayol, {J}. {L}. and {F}ardeau, {M}arie-{L}aure},
  editor = {},
  language = {{ENG}},
  abstract = {{T}he present study investigates the purification and biochemical characterization of an extracellular thermostable xylanase (called {XYN}35) from {C}aldicoprobacter algeriensis sp. nov., strain {TH}7{C}1({T}), a thermophilic, anaerobic strain isolated from the hydrothermal hot spring of {G}uelma ({A}lgeria). {T}he maximum xylanase activity recorded after 24 h of incubation at 70 degrees {C} and in an optimized medium containing 10 g/{L} mix birchwood-and oats spelt-xylan was 250 {U}/m{L}. {T}he pure protein was obtained after heat treatment (1 h at 70 degrees {C}), followed by sequential column chromatographies on {S}ephacryl {S}-200 gel filtration and {M}ono-{S} {S}epharose anion-exchange. {M}atrix assisted laser desorption ionization-time of flight mass spectrometry ({MALDI}-{TOF}/{MS}) analysis indicated that the purified enzyme is a monomer with a molecular mass of 35,075.10 {D}a. {T}he results from amino-acid sequence analysis revealed high homology between the 21 {NH}2-terminal residues of {XYN}35 and those of bacterial xylanases. {T}he enzyme showed optimum activity at p{H} 11 and 70 degrees {C}. {W}hile {XYN}35 was activated by {C}a2+, {M}n2+, and {M}g2+, it was completely inhibited by {H}g2+ and {C}d2+. {T}he xylanase showed higher specific activity on soluble oat-spelt xylan, followed by beechwood xylan. {T}his enzyme was also noted to obey the {M}ichaelis-{M}enten kinetics, with {K}m and kcat values on oat-spelt xylan being 1.33 mg/m{L} and 400 min(-1), respectively. {T}hin-layer chromatography soluble oat-spelt xylan ({TLC}) analysis showed that the final hydrolyzed products of the enzyme from birchwood xylan were xylose, xylobiose, and xylotriose. {T}aken together, the results indicated that the {XYN}35 enzyme has a number of attractive biochemical properties that make it a potential promising candidate for future application in the pulp bleaching industry.},
  keywords = {{C}aldicoprobacter algeriensis ; {X}ylanase ; {P}urification ; {H}ydrolytic pattern ; {P}ulp bleaching industry ; {ALGERIE}},
  booktitle = {},
  journal = {{C}arbohydrate {R}esearch},
  volume = {419},
  numero = {},
  pages = {60--68},
  ISSN = {0008-6215},
  year = {2016},
  DOI = {10.1016/j.carres.2015.10.013},
  URL = {https://www.documentation.ird.fr/hor/fdi:010066074},
}