Source:http://linkedlifedata.com/resource/pubmed/id/19458917
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2009-8-5
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pubmed:abstractText |
A recombinant putative beta-galactosidase from Thermoplasma acidophilum was purified as a single 57 kDa band of 82 U mg(-1). The molecular mass of the native enzyme was 114 kDa as a dimer. Maximum activity was observed at pH 6.0 and 90 degrees C. The enzyme was unstable below pH 6.0: at pH 6 its half-life at 75 degrees C was 28 days but at pH 4.5 was only 13 h. Catalytic efficiencies decreased as p-nitrophenyl(pNP)-beta-D-fucopyranoside (1067) > pNP-beta-D-glucopyranoside (381) > pNP-beta-D-galactopyranoside (18) > pNP-beta-D-mannopyranoside (11 s(-1) mM(-1)), indicating that the enzyme was a beta-glycosidase.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1573-6776
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1457-62
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pubmed:meshHeading |
pubmed-meshheading:19458917-Archaeal Proteins,
pubmed-meshheading:19458917-Dimerization,
pubmed-meshheading:19458917-Enzyme Stability,
pubmed-meshheading:19458917-Half-Life,
pubmed-meshheading:19458917-Hydrogen-Ion Concentration,
pubmed-meshheading:19458917-Molecular Weight,
pubmed-meshheading:19458917-Recombinant Proteins,
pubmed-meshheading:19458917-Substrate Specificity,
pubmed-meshheading:19458917-Temperature,
pubmed-meshheading:19458917-Thermoplasma,
pubmed-meshheading:19458917-beta-Glucosidase
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pubmed:year |
2009
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pubmed:articleTitle |
Characterization of an acid-labile, thermostable beta-glycosidase from Thermoplasma acidophilum.
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pubmed:affiliation |
Department of Bioscience and Biotechnology, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul 143-701, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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