Source:http://linkedlifedata.com/resource/pubmed/id/11004558
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2000-10-30
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pubmed:abstractText |
The effects of aqueous surfactant solutions on the kinetics and stability of cutinase from Fusarium solani pisi were studied. The surfactant sodium bis[2-ethylhexyl]ester sulfosuccinic acid (AOT) acts as a pseudo-competitive inhibitor within a limited concentration range relative to the hydrolysis of short-chain p-nitrophenyl esters. For higher concentrations a hyperbolic mixed inhibition takes place. A pseudo-activation of hydrolysis in presence of AOT and hexadecyltrimethyl-ammonium bromide (CTAB) was observed. CTAB has similar effects on kinetics of cutinase. Cutinase revealed to be stable in CTAB solutions, with activity retention as high as 80%. AOT has a deleterious effect on the enzyme in the time course, resulting in acute loss of activity possibly related with unfolding of the protein structure. A relation between deactivation rate constants and AOT/cutinase concentration ratios is suggested. The presence of the linear alcohol, 1-hexanol, was included in these solutions, in the attempt to interpret the deactivation of cutinase when encapsulated in reversed micelle systems in the absence of this co-surfactant.
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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/Carboxylic Ester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Ions,
http://linkedlifedata.com/resource/pubmed/chemical/Micelles,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Surface-Active Agents,
http://linkedlifedata.com/resource/pubmed/chemical/cutinase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
1480
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
92-106
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11004558-Carboxylic Ester Hydrolases,
pubmed-meshheading:11004558-Enzyme Stability,
pubmed-meshheading:11004558-Ions,
pubmed-meshheading:11004558-Kinetics,
pubmed-meshheading:11004558-Micelles,
pubmed-meshheading:11004558-Recombinant Proteins,
pubmed-meshheading:11004558-Surface Tension,
pubmed-meshheading:11004558-Surface-Active Agents
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pubmed:year |
2000
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pubmed:articleTitle |
Effects of ionic surfactants used in reversed micelles on cutinase activity and stability.
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pubmed:affiliation |
Centro de Engenharia Biológica e Química, Instituto Superior Técnico, Lisbon, Portugal. p1073@alfa.ist.utl.pt
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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