| pubmed-article:11179657 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11179657 | lifeskim:mentions | umls-concept:C0023764 | lld:lifeskim |
| pubmed-article:11179657 | lifeskim:mentions | umls-concept:C0220908 | lld:lifeskim |
| pubmed-article:11179657 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:11179657 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11179657 | pubmed:dateCreated | 2001-2-22 | lld:pubmed |
| pubmed-article:11179657 | pubmed:abstractText | Various soil samples were collected to screen the presence of microorganisms which have ability to degrade TOE. One strain (AKU-883) with good TOE degrading activity was isolated and identified as Burkholderia cepacia and the extracellular enzyme was purified to homogeneity. The purification was achieved by ultrafiltration, Super Q anion-exchange chromatography and Superdex 200HR gel-filtration in the presence of Triton X. The enzyme was purified to 85-fold, and specific activity of 4.910 kU mg protein(-1). The peak preparation on gel filtration showed a single band of 34 kDa on SDS-PAGE and native PAGE which indicate the monomeric nature of the enzyme. The pI of the enzyme was 6.3. The enzyme showed the maximum activity at pH 9 and 65 degrees C, and was stable in the range of pH 5--10 and up to 60 degrees C. Almost all the activity (92%) was kept after incubation for more than 1 week at 50 degrees C (pH 7.3). High activities remained even in water-miscible solvents such as ethanol, dimethyl formamide, diisopropyl ether, and dioxane. The N-terminal 16 amino acid residues were determined as A-N-G-Y-A-A-T-R-Y-P-I-I-L-V-G-G, which showed a consensus sequence for lipases from Burkholderia species. Thus the enzyme was concluded to be a kind of lipase. | lld:pubmed |
| pubmed-article:11179657 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11179657 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11179657 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11179657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11179657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11179657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11179657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11179657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11179657 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11179657 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11179657 | pubmed:issn | 0378-1097 | lld:pubmed |
| pubmed-article:11179657 | pubmed:author | pubmed-author:SugimotoMM | lld:pubmed |
| pubmed-article:11179657 | pubmed:author | pubmed-author:KawaiFF | lld:pubmed |
| pubmed-article:11179657 | pubmed:author | pubmed-author:IshimotoRR | lld:pubmed |
| pubmed-article:11179657 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11179657 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:11179657 | pubmed:volume | 195 | lld:pubmed |
| pubmed-article:11179657 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11179657 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11179657 | pubmed:pagination | 231-5 | lld:pubmed |
| pubmed-article:11179657 | pubmed:meshHeading | pubmed-meshheading:11179657... | lld:pubmed |
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| pubmed-article:11179657 | pubmed:meshHeading | pubmed-meshheading:11179657... | lld:pubmed |
| pubmed-article:11179657 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11179657 | pubmed:articleTitle | Screening and characterization of trehalose-oleate hydrolyzing lipase. | lld:pubmed |
| pubmed-article:11179657 | pubmed:affiliation | Research Institute for Bioresources, Okayama University, 2-20-1 Chuo, Kurashiki 710-0046, Japan. ishimoto@rib.okayama-u.ac.jp | lld:pubmed |
| pubmed-article:11179657 | pubmed:publicationType | Journal Article | lld:pubmed |
