Source:http://linkedlifedata.com/resource/pubmed/id/18499049
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2008-5-23
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pubmed:abstractText |
A novel cholesterol esterase with there and throughout to synthesisze steryl ester was obtained from the culture filtrate of a fungal strain Trichoderma sp. AS59 isolated from soil. The extracellular enzyme was a monomeric protein with a molecular mass of approximately 58 kDa and an isoelectric point of 4.3. The optimal temperature was between 35 degrees C and 40 degrees C, and the optimal pH was 7.0. The enzyme retained 75% of the initial activity after 18 h of incubation at 30 degrees C in the pH range of 3.5-7.5. Its relative hydrolytic activities on fatty acid cholesteryl esters were in the following order: butyrate (121%), linoleate (100%), caprylate (79%), myristate (42%), palmitate (38%), caproate (37%), and laurate (35%). Unlike mammalian pancreatic cholesterol esterase that is activated by primary cholates on hydrolysis of long-chain fatty acid cholesteryl esters, the enzyme from Trichoderma sp. AS59 displayed its basal activity and was not affected by cholate up to a concentration of 5 mM. At higher cholate concentrations the activity gradually decreased, but reincreased at about 40 mM to reach more than twice the basal activity at 100 mM. The enzyme exhibited a broad substrate specificity, being capable of hydrolyzing various fatty acid esters of not only cholesterol, but also methanol, glycerol, and p-nitrophenol. When incubated with a mixture of cholesterol and oleic acid of equal amounts, the enzyme achieved stoichiometrical esterification in 5 h, indicating its potential utility in food additives and liquid crystal devices.
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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/Cholates,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oleic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Sterol Esterase
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1389-1723
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
341-9
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pubmed:meshHeading |
pubmed-meshheading:18499049-Cholates,
pubmed-meshheading:18499049-Cholesterol,
pubmed-meshheading:18499049-Cholesterol Esters,
pubmed-meshheading:18499049-Fungal Proteins,
pubmed-meshheading:18499049-Oleic Acid,
pubmed-meshheading:18499049-Sterol Esterase,
pubmed-meshheading:18499049-Substrate Specificity,
pubmed-meshheading:18499049-Trichoderma
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pubmed:year |
2008
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pubmed:articleTitle |
Characterization of novel cholesterol esterase from Trichoderma sp. AS59 with high ability to synthesize steryl esters.
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pubmed:affiliation |
Faculty of Engineering, Tokushima Bunri University, 1314-1 Shido, Sanuki 769-2193, Japan. maeda@fe.bunri-u.ac.jp
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pubmed:publicationType |
Journal Article
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