Source:http://linkedlifedata.com/resource/pubmed/id/18668373
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2009-7-2
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pubmed:abstractText |
A thermostable xylanase from a newly isolated thermophilic fungus Talaromyces thermophilus was purified and characterized. The enzyme was purified to homogeneity by ammonium sulfate precipitation, diethylaminoethyl cellulose anion exchange chromatography, P-100 gel filtration, and Mono Q chromatography with a 23-fold increase in specific activity and 17.5% recovery. The molecular weight of the xylanase was estimated to be 25 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration. The enzyme was highly active over a wide range of pH from 4.0 to 10.0. The relative activities at pH5.0, 9.0, and 10.0 were about 80%, 85.0%, and 60% of that at pH7.5, respectively. The optimum temperature of the purified enzyme was 75 degrees C. The enzyme showed high thermal stability at 50 degrees C (7 days) and the half-life of the xylanase at 100 degrees C was 60 min. The enzyme was free from cellulase activity. K (m) and V (max) values at 50 degrees C of the purified enzyme for birchwood xylan were 22.51 mg/ml and 1.235 micromol min(-1) mg(-1), respectively. The enzyme was activated by Ag(+), Co(2+), and Cu(2+); on the other hand, Hg(2+), Ba(2+), and Mn(2+) inhibited the enzyme. The present study is among the first works to examine and describe a secreted, cellulase-free, and highly thermostable xylanase from the T. thermophilus fungus whose application as a pre-bleaching aid is of apparent importance for pulp and paper industries.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DEAE-Cellulose,
http://linkedlifedata.com/resource/pubmed/chemical/Endo-1,4-beta Xylanases,
http://linkedlifedata.com/resource/pubmed/chemical/Mono Q,
http://linkedlifedata.com/resource/pubmed/chemical/Resins, Synthetic,
http://linkedlifedata.com/resource/pubmed/chemical/Xylans
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1559-0291
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
158
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
200-12
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pubmed:meshHeading |
pubmed-meshheading:18668373-Chromatography, Gel,
pubmed-meshheading:18668373-Chromatography, Ion Exchange,
pubmed-meshheading:18668373-DEAE-Cellulose,
pubmed-meshheading:18668373-Endo-1,4-beta Xylanases,
pubmed-meshheading:18668373-Enzyme Stability,
pubmed-meshheading:18668373-Hydrolysis,
pubmed-meshheading:18668373-Kinetics,
pubmed-meshheading:18668373-Resins, Synthetic,
pubmed-meshheading:18668373-Talaromyces,
pubmed-meshheading:18668373-Temperature,
pubmed-meshheading:18668373-Xylans
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pubmed:year |
2009
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pubmed:articleTitle |
Highly thermostable xylanase of the thermophilic fungus Talaromyces thermophilus: purification and characterization.
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pubmed:affiliation |
Laboratoire de Génétique Moléculaire des Eucaryotes, Centre de Biotechnologie de Sfax, Sfax, Tunisia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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