| Highly thermostable xylanase of the thermophilic fungus Talaromyces thermophilus: purification and characterization. | |
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MedLine Citation:
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PMID: 18668373 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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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Authors:
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Ines Maalej; Ines Belhaj; Najla Fourati Masmoudi; Hafedh Belghith |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-07-31 |
Journal Detail:
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Title: Applied biochemistry and biotechnology Volume: 158 ISSN: 1559-0291 ISO Abbreviation: Appl. Biochem. Biotechnol. Publication Date: 2009 Jul |
Date Detail:
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Created Date: 2009-07-02 Completed Date: 2009-10-01 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8208561 Medline TA: Appl Biochem Biotechnol Country: United States |
Other Details:
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Languages: eng Pagination: 200-12 Citation Subset: IM |
Affiliation:
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Laboratoire de Génétique Moléculaire des Eucaryotes, Centre de Biotechnologie de Sfax, Sfax, Tunisia. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Chromatography, Gel Chromatography, Ion Exchange DEAE-Cellulose Endo-1,4-beta Xylanases / biosynthesis, chemistry, isolation & purification*, metabolism* Enzyme Stability Hydrolysis Kinetics Resins, Synthetic Talaromyces / enzymology*, metabolism Temperature Xylans / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Resins, Synthetic; 0/Xylans; 83453-40-1/Mono Q; 9013-34-7/DEAE-Cellulose; EC 3.2.1.8/Endo-1,4-beta Xylanases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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