Source:http://linkedlifedata.com/resource/pubmed/id/10099579
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1999-4-26
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pubmed:abstractText |
A lipase from Candida cylindracea immobilized by adsorption on microporous polypropylene fibers was used to selectively hydrolyze the saturated and monounsaturated fatty acid residues of menhaden oil at 40 degrees C and pH 7.0. At a space time of 3.5 h, the shell and tube reactor containing these hollow fibers gives a fractional release of each of the saturated and monounsaturated fatty acid residues (i.e., C14, C16, C16:1, C18:1) of ca. 88% of the corresponding possible asymptotic value. The corresponding coproduct glycerides retained over 90% of the initial residues of both eicosapentaenoic (EPA; C20:5) and docosahexaenoic (DHA; C22:6) acids. The half-life of the immobilized lipase was 170 h when the reactor was operated at the indicated (optimum) conditions. Rate expressions associated with a generic ping-pong bi-bi mechanism were used to fit the experimental data for the lipase catalyzed reaction. Both uni- and multiresponse nonlinear regression methods were employed to determine the kinetic parameters associated with these rate expressions. The best statistical fit of the uniresponse data was obtained for a rate expression, which is formally equivalent to a general Michaelis-Menten mechanism. After reparameterization, this rate expression reduced to a pseudo-first-order model. For the multiresponse analysis, a model that employed a normal distribution of the ratio of Vmax/Km with respect to the chain length of the fatty acid residues provided the best statistical fit of the experimental data.
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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/Docosahexaenoic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Eicosapentaenoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes, Immobilized,
http://linkedlifedata.com/resource/pubmed/chemical/Fish Oils,
http://linkedlifedata.com/resource/pubmed/chemical/Lipase,
http://linkedlifedata.com/resource/pubmed/chemical/Menhaden oil
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-3592
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1999 John Wiley & Sons, Inc.
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33-45
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10099579-Bioreactors,
pubmed-meshheading:10099579-Biotechnology,
pubmed-meshheading:10099579-Candida,
pubmed-meshheading:10099579-Docosahexaenoic Acids,
pubmed-meshheading:10099579-Eicosapentaenoic Acid,
pubmed-meshheading:10099579-Enzymes, Immobilized,
pubmed-meshheading:10099579-Fish Oils,
pubmed-meshheading:10099579-Hydrogen-Ion Concentration,
pubmed-meshheading:10099579-Hydrolysis,
pubmed-meshheading:10099579-Kinetics,
pubmed-meshheading:10099579-Lipase,
pubmed-meshheading:10099579-Regression Analysis,
pubmed-meshheading:10099579-Time Factors
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pubmed:year |
1999
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pubmed:articleTitle |
Hydrolysis of menhaden oil by a Candida cylindracea lipase immobilized in a hollow-fiber reactor.
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pubmed:affiliation |
Department of Chemical Engineering, University of Wisconsin, 1415 Engineering Drive, Madison, Wisconsin 53706, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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