Source:http://linkedlifedata.com/resource/pubmed/id/12147262
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2002-7-30
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| pubmed:abstractText |
A major extracellular endoglucanase purified to homogeneity from Thermoascus aurantiacus had a M(r) of 34 kDa and a pI of 3.7 and was optimally active at 70-80 degrees C and pH 4.0-4.4. It was stable at pH 2.8-6.8 at 50 degrees C for 48 h and maintained its secondary structure and folded conformation up to 70 degrees C at pH 5.0 and 2.8, respectively. A 33-amino acid sequence at the N terminus showed considerable homology with 14 microbial endoglucanases having highly conserved 8 amino acids (positions 10-17) and Gly, Pro, Gly, and Pro at positions 8, 22, 23, and 32, respectively. The enzyme is rich in Asp (15%) and Glu (10%) with a carbohydrate content of 2.7%. Polyclonal antibodies of endoglucanase cross-reacted with their own antigen and with other purified cellulases from T. aurantiacus. The endoglucanase was specific for polymeric substrates with highest activity toward carboxymethyl cellulose followed by barley beta-glucan and lichenan. It preferentially cleaved the internal glycosidic bonds of Glc(n) and MeUmbGlc(n) and possessed an extended substrate-binding site with five subsites. The data indicate that the endoglucanase from T. aurantiacus is a member of glycoside hydrolase family 5.
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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 |
Aug
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| pubmed:issn |
0003-9861
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2002 Elsevier Science (USA).
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| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
404
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
243-53
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:12147262-Ascomycota,
pubmed-meshheading:12147262-Calorimetry, Differential Scanning,
pubmed-meshheading:12147262-Carboxymethylcellulose Sodium,
pubmed-meshheading:12147262-Cellulase,
pubmed-meshheading:12147262-Chromatography, High Pressure Liquid,
pubmed-meshheading:12147262-Enzyme Activation,
pubmed-meshheading:12147262-Enzyme Stability,
pubmed-meshheading:12147262-Extracellular Space,
pubmed-meshheading:12147262-Glucans,
pubmed-meshheading:12147262-Hydrogen-Ion Concentration,
pubmed-meshheading:12147262-Molecular Sequence Data,
pubmed-meshheading:12147262-Protein Conformation,
pubmed-meshheading:12147262-Protein Folding,
pubmed-meshheading:12147262-Protein Structure, Secondary,
pubmed-meshheading:12147262-Sequence Analysis, Protein,
pubmed-meshheading:12147262-Sequence Homology, Amino Acid,
pubmed-meshheading:12147262-Substrate Specificity,
pubmed-meshheading:12147262-Temperature,
pubmed-meshheading:12147262-Thermodynamics
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| pubmed:year |
2002
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| pubmed:articleTitle |
Biochemical characterization and mode of action of a thermostable endoglucanase purified from Thermoascus aurantiacus.
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| pubmed:affiliation |
Food Materials Science Division, Institute of Food Research, Norwich Research Park, Colney, Norwich, NR4 7UA, UK.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|