Source:http://linkedlifedata.com/resource/pubmed/id/11179657
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2001-2-22
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Lipase,
http://linkedlifedata.com/resource/pubmed/chemical/Oleic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Solvents,
http://linkedlifedata.com/resource/pubmed/chemical/Trehalose
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0378-1097
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
195
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
231-5
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pubmed:meshHeading |
pubmed-meshheading:11179657-Amino Acid Sequence,
pubmed-meshheading:11179657-Burkholderia cepacia,
pubmed-meshheading:11179657-Catalysis,
pubmed-meshheading:11179657-Enzyme Stability,
pubmed-meshheading:11179657-Esters,
pubmed-meshheading:11179657-Hydrogen-Ion Concentration,
pubmed-meshheading:11179657-Hydrolysis,
pubmed-meshheading:11179657-Lipase,
pubmed-meshheading:11179657-Molecular Sequence Data,
pubmed-meshheading:11179657-Oleic Acid,
pubmed-meshheading:11179657-Soil Microbiology,
pubmed-meshheading:11179657-Solvents,
pubmed-meshheading:11179657-Temperature,
pubmed-meshheading:11179657-Trehalose
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pubmed:year |
2001
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pubmed:articleTitle |
Screening and characterization of trehalose-oleate hydrolyzing lipase.
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pubmed:affiliation |
Research Institute for Bioresources, Okayama University, 2-20-1 Chuo, Kurashiki 710-0046, Japan. ishimoto@rib.okayama-u.ac.jp
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pubmed:publicationType |
Journal Article
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