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Talaromyces thermophilus beta-D-xylosidase: purification, characterization and xylobiose synthesis.

Identifieur interne : 000726 ( Main/Exploration ); précédent : 000725; suivant : 000727

Talaromyces thermophilus beta-D-xylosidase: purification, characterization and xylobiose synthesis.

Auteurs : Mohamed Guerfali [Tunisie] ; Ali Gargouri ; Hafedh Belghith

Source :

RBID : pubmed:18592411

Descripteurs français

English descriptors

Abstract

When grown on wheat bran as the only carbon source, the filamentous fungus Talaromyces thermophilus produces large amounts of beta-xylosidase activity. The presence of glucose drastically decreases the beta-xylosidase production level. The beta-xylosidase of T. thermophilus was purified by ammonium sulfate precipitation, DEAE-cellulose chromatography, and gel filtration (high-performance liquid chromatography). The molecular mass of the enzyme was estimated to be 97 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration. The enzyme activity was optimum at 50 degrees C and pH 7. The apparent Michaelis constant K(m) of the beta-xylosidase was 2.37 mM for p-nitrophenyl-beta-D-xylopyranoside, with a V(max) of 0.049 micromol min(-1) per milligram protein. Enzyme activity was inhibited by Cu(2+), Hg(2+), and Zn(2+) and activated by Ca(2+), Mn(2+), and Co(+) at a concentration of 5 mM. At high xylose concentration, this enzyme catalyses the condensation reaction leading to xylobiose production.

DOI: 10.1007/s12010-008-8260-x
PubMed: 18592411


Affiliations:


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<term>Chromatography, High Pressure Liquid</term>
<term>Cobalt (pharmacology)</term>
<term>Copper (pharmacology)</term>
<term>Disaccharides (biosynthesis)</term>
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<term>Fungal Proteins (metabolism)</term>
<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Manganese (pharmacology)</term>
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<term>Activation enzymatique ()</term>
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<term>Chromatographie</term>
<term>Chromatographie en phase liquide à haute performance</term>
<term>Chromatographie sur gel</term>
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<term>Cobalt (pharmacologie)</term>
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<term>Température</term>
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<term>Xylosidases (isolement et purification)</term>
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<term>Chromatography</term>
<term>Chromatography, Gel</term>
<term>Chromatography, High Pressure Liquid</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Molecular Weight</term>
<term>Temperature</term>
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<div type="abstract" xml:lang="en">When grown on wheat bran as the only carbon source, the filamentous fungus Talaromyces thermophilus produces large amounts of beta-xylosidase activity. The presence of glucose drastically decreases the beta-xylosidase production level. The beta-xylosidase of T. thermophilus was purified by ammonium sulfate precipitation, DEAE-cellulose chromatography, and gel filtration (high-performance liquid chromatography). The molecular mass of the enzyme was estimated to be 97 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration. The enzyme activity was optimum at 50 degrees C and pH 7. The apparent Michaelis constant K(m) of the beta-xylosidase was 2.37 mM for p-nitrophenyl-beta-D-xylopyranoside, with a V(max) of 0.049 micromol min(-1) per milligram protein. Enzyme activity was inhibited by Cu(2+), Hg(2+), and Zn(2+) and activated by Ca(2+), Mn(2+), and Co(+) at a concentration of 5 mM. At high xylose concentration, this enzyme catalyses the condensation reaction leading to xylobiose production.</div>
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