Source:http://linkedlifedata.com/resource/pubmed/id/15322773
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-11-19
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pubmed:abstractText |
A fungal strain, C-4, was isolated from etiolated leaves. Based on taxonomic studies, the fungus C-4 can be classified as a strain of Trichoderma species. When strain C-4 was cultured in Mandels' medium at 28 degrees C for 6 days, the enzyme activities detected in the broth corresponded to 8.2 U/ml (28.1 U/mg) carboxymethylcellulase activity. An endoglucanase (EG; F-I-II) was purified from the culture filtrate of the strain through a four-step procedure-chromatography on Sephacryl S-200, DEAE-Sephadex A-50, Con A-Sepharose, and Chromatofocusing on Mono-P (HPLC). The molecular weight of this EG, which was called C4endoII, was determined to be about 51 kDa. The optimum temperature and pH of C4endoII were 50 degrees C and 5.0, respectively. Incubation at 50 degrees C for 24 h did not destroy the cellulose degradation activity. Amino acid sequence analysis revealed the N-terminal sequence of an internal peptide of C4endoII to be Phe-Ala-Gly-Ile-Asn-Ile-Ala-Gly-Phe-Asp-Phe, which is homologous to EGII from Trichoderma reesei. A C4endoII cDNA (C4endoII) was cloned from a cDNA library constructed using the mRNA of the strain cultivated in a cellulase-induction medium. The deduced protein sequence of C4endoII was 417 amino acids long and had a putative signal sequence of 21 amino acids with a predicted cleavage site after Ala-21. A single potential N-glycosylation site was present in the amino acid sequence.
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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 |
Nov
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pubmed:issn |
0175-7598
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
63-70
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15322773-Amino Acid Sequence,
pubmed-meshheading:15322773-Cellulase,
pubmed-meshheading:15322773-Cloning, Molecular,
pubmed-meshheading:15322773-Hydrogen-Ion Concentration,
pubmed-meshheading:15322773-Molecular Sequence Data,
pubmed-meshheading:15322773-Sequence Alignment,
pubmed-meshheading:15322773-Species Specificity,
pubmed-meshheading:15322773-Temperature,
pubmed-meshheading:15322773-Time Factors,
pubmed-meshheading:15322773-Trichoderma
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pubmed:year |
2004
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pubmed:articleTitle |
Characterization and molecular cloning of a novel endoglucanase from Trichoderma sp. C-4.
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pubmed:affiliation |
Department of Biological Science, University of Ulsan, 680-749 Ulsan, South Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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