| pubmed-article:9797302 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9797302 | lifeskim:mentions | umls-concept:C0004594 | lld:lifeskim |
| pubmed-article:9797302 | lifeskim:mentions | umls-concept:C0053413 | lld:lifeskim |
| pubmed-article:9797302 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:9797302 | lifeskim:mentions | umls-concept:C0162326 | lld:lifeskim |
| pubmed-article:9797302 | lifeskim:mentions | umls-concept:C0917792 | lld:lifeskim |
| pubmed-article:9797302 | lifeskim:mentions | umls-concept:C0598888 | lld:lifeskim |
| pubmed-article:9797302 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:9797302 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:9797302 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:9797302 | pubmed:dateCreated | 1999-1-14 | lld:pubmed |
| pubmed-article:9797302 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9797302 | pubmed:abstractText | A DNA genomic library constructed from Bacillus stearothermophilus, a gram-positive, facultative thermophilic aerobe that secretes a thermostable beta-mannanase, was screened for mannan hydrolytic activity. Recombinant beta-mannanase activity was detected on the basis of the clearing of halos around Escherichia coli colonies grown on a dye-labelled substrate, Remazol brilliant blue-locust bean gum. The nucleotide sequence of the mannanase gene, manF, corresponded to an open reading frame of 2,085 bp that codes for a 32-amino-acid signal peptide and a mature protein with a molecular mass of 76,089 Da. From sequence analysis, ManF belongs to glycosyl hydrolase family 5 and exhibits higher similarity to eukaryotic than to bacterial mannanases. The manF coding sequence was subcloned into the pH6EX3 expression plasmid and expressed in E. coli as a recombinant fusion protein containing a hexahistidine N-terminal sequence. The fusion protein has thermostability similar to the native enzyme and was purified by Ni2+ affinity chromatography. The values for the kinetic parameters Vmax and Km were 384 U/mg and 2.4 mg/ml, respectively, for the recombinant mannanase and were comparable to those of the native enzyme. | lld:pubmed |
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| pubmed-article:9797302 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9797302 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9797302 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9797302 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9797302 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9797302 | pubmed:issn | 0099-2240 | lld:pubmed |
| pubmed-article:9797302 | pubmed:author | pubmed-author:TalbotGG | lld:pubmed |
| pubmed-article:9797302 | pubmed:author | pubmed-author:SyguschJJ | lld:pubmed |
| pubmed-article:9797302 | pubmed:author | pubmed-author:EthierNN | lld:pubmed |
| pubmed-article:9797302 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9797302 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:9797302 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9797302 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9797302 | pubmed:pagination | 4428-32 | lld:pubmed |
| pubmed-article:9797302 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9797302 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9797302 | pubmed:articleTitle | Gene cloning, DNA sequencing, and expression of thermostable beta-mannanase from Bacillus stearothermophilus. | lld:pubmed |
| pubmed-article:9797302 | pubmed:affiliation | Département de Biochimie, Faculté de Médecine, Université de Montréal, Montréal, Québec, Canada H3C 3J7. | lld:pubmed |
| pubmed-article:9797302 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9797302 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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