ABSTRACT: This paper reports a kinetic model for the self-epoxidation of oleic acid with toluene as solvent and Novozym 435 (a commercially available preparation of immobilized Can-dida antarctica lipase) as catalyst at 30°C. The effects of various parameters on the conversion and rates of reaction...

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http://lib3.dss.go.th/fulltext/Journal/J.AOCS/J.AOCS/2001/no.4/2001v78n4p347-351.pdf
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spelling ftciteseerx:oai:CiteSeerX.psu:10.1.1.462.5085 2023-05-15T14:06:38+02:00 The Pennsylvania State University CiteSeerX Archives application/pdf http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.462.5085 http://lib3.dss.go.th/fulltext/Journal/J.AOCS/J.AOCS/2001/no.4/2001v78n4p347-351.pdf en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.462.5085 http://lib3.dss.go.th/fulltext/Journal/J.AOCS/J.AOCS/2001/no.4/2001v78n4p347-351.pdf Metadata may be used without restrictions as long as the oai identifier remains attached to it. http://lib3.dss.go.th/fulltext/Journal/J.AOCS/J.AOCS/2001/no.4/2001v78n4p347-351.pdf mobilized lipase text ftciteseerx 2016-10-16T00:04:39Z ABSTRACT: This paper reports a kinetic model for the self-epoxidation of oleic acid with toluene as solvent and Novozym 435 (a commercially available preparation of immobilized Can-dida antarctica lipase) as catalyst at 30°C. The effects of various parameters on the conversion and rates of reaction were stud-ied. Both the initial rate and the progress curve data were used to fit an ordered bi-bi model. At low temperatures, the rate of epoxidation was faster than the rate of deactivation of the en-zyme by hydrogen peroxide. Text Antarc* Antarctica Unknown
institution Open Polar
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description ABSTRACT: This paper reports a kinetic model for the self-epoxidation of oleic acid with toluene as solvent and Novozym 435 (a commercially available preparation of immobilized Can-dida antarctica lipase) as catalyst at 30°C. The effects of various parameters on the conversion and rates of reaction were stud-ied. Both the initial rate and the progress curve data were used to fit an ordered bi-bi model. At low temperatures, the rate of epoxidation was faster than the rate of deactivation of the en-zyme by hydrogen peroxide.
author2 The Pennsylvania State University CiteSeerX Archives
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