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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1991-3-27
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pubmed:abstractText |
An aryl beta-xylosidase was purified to homogeneity from an Escherichia coli strain containing a recombinant plasmid carrying a beta-xylosidase (EC 3.2.1.37) gene from the extremely thermophilic anaerobic bacterium isolate Tp8T6.3.3.1 ('Caldocellum saccharolyticum'). It has a pI of 4.3 and shows optimal activity at pH 5.7. The enzyme is highly specific, acting on o- and p-nitrophenyl beta-D-xylopyranosides and minimally on p-nitrophenyl alpha-L-arabinopyranoside. It does not act on xylobiose. The Km for p-nitrophenyl beta-D-xylopyranoside at the optimum pH for activity is 10 mM, and at pH 7.0 is 6.7 mM. Xylose is a competitive inhibitor with Ki 40 mM. Thermal inactivation follows first-order kinetics at 65 and 70 degrees C with t1/2 values of 4.85 h and 40 min respectively. The t1/2 at 70 degrees C is increased 3-fold and 4-fold by the addition of 0.5 mg of BSA/ml and 2 mM-dithiothreitol respectively.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-16347038,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-16347313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-16347327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-17789813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-2111111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-2985470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-3117033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-3314899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-4634162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-5791586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-6421572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-6435537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-6808312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847618-942051
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
273 ( Pt 3)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
645-50
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pubmed:dateRevised |
2010-9-9
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pubmed:meshHeading |
pubmed-meshheading:1847618-Bacteria, Anaerobic,
pubmed-meshheading:1847618-Chromatography,
pubmed-meshheading:1847618-Chromatography, Gel,
pubmed-meshheading:1847618-Chromatography, Ion Exchange,
pubmed-meshheading:1847618-Durapatite,
pubmed-meshheading:1847618-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1847618-Enzyme Stability,
pubmed-meshheading:1847618-Escherichia coli,
pubmed-meshheading:1847618-Glycoside Hydrolases,
pubmed-meshheading:1847618-Hot Temperature,
pubmed-meshheading:1847618-Hydroxyapatites,
pubmed-meshheading:1847618-Kinetics,
pubmed-meshheading:1847618-Recombinant Proteins,
pubmed-meshheading:1847618-Xylan Endo-1,3-beta-Xylosidase,
pubmed-meshheading:1847618-Xylosidases
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pubmed:year |
1991
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pubmed:articleTitle |
Purification and properties of an aryl beta-xylosidase from a cellulolytic extreme thermophile expressed in Escherichia coli.
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pubmed:affiliation |
Microbial Biochemistry and Biotechnology Research Unit, University of Waikato, Hamilton, New Zealand.
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pubmed:publicationType |
Journal Article
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