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Factors affecting the esterification of lauric acid using an immobilized biocatalyst: enzyme characterization and studies in a well-mixed reactor

The esterification of lauric acid with geraniol catalyzed by the commercially immobilized lipase preparation from Mucor miehei, Lipozyme(®), was studied in well-stirred flasks. The enzyme support was characterized in terms of its internal and external surface area, protein location, and protein cont...

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Main Authors: Vazquez-Lima, F., Pyle, D. L., Asenjo, J.A.
Format: Article
Language:English
Published: John Wiley & Sons, Inc. 2010
Subjects:
esterification
lauric acid
geraniol
lipozyme
Online Access:http://dspace.unimap.edu.my/xmlui/handle/123456789/9238
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spelling my.unimap-92382010-08-30T05:34:25Z Factors affecting the esterification of lauric acid using an immobilized biocatalyst: enzyme characterization and studies in a well-mixed reactor Vazquez-Lima, F. Pyle, D. L. Asenjo, J.A. esterification lauric acid geraniol lipozyme The esterification of lauric acid with geraniol catalyzed by the commercially immobilized lipase preparation from Mucor miehei, Lipozyme(®), was studied in well-stirred flasks. The enzyme support was characterized in terms of its internal and external surface area, protein location, and protein content. It was found that the enzyme was mainly located on the external surface of the support, therefore, internal diffusional limitations were not important. It was also shown that the protein content of the support depends on the size of the particle, with smaller particles containing higher amounts of protein per unit weight. Under the conditions studied, the reaction was not under external mass transfer limitations, and the initial reaction rate depended on the size of the support particles. This was mainly due to the different protein contents on the support as a function of particle size and not to internal or external mass transfer limitations. Also, it was found that the inhibition exerted by water was predominantly a physical effect due to its accumulation around the enzyme. It was also found that the reaction was substrate inhibited by lauric acid, but not by geraniol. The esterification of lauric acid with geraniol catalyzed by the commercially immobilized lipase preparation from Mucor miehei, Lipozyme, was studied in well-stirred flasks. The enzyme support was characterized in terms of its internal and external surface area, protein location, and protein content. It was found that the enzyme was mainly located on the external surface of the support, therefore, internal diffusional limitations were not important. It was also shown that the protein content of the support depends on the size of the particle, with smaller particles containing higher amounts of protein per unit weight. Under the conditions studied, the reaction was not under external mass transfer limitations, and the initial reaction rate depended on the size of the support particles. This was mainly due to the different protein contents on the support as a function of particle size and not to internal or external mass transfer limitations. Also, it was found that the inhibition exerted by water was predominantly a physical effect due to its accumulation around the enzyme. It was also found that the reaction was substrate inhibited by lauric acid, but not by geraniol. 2010-08-30T05:34:25Z 2010-08-30T05:34:25Z 1995-04-05 Article Biotechnology and Bioengineering, vol. 46, issue 1, 1995, pages 69-79 0006-3592 0006-3592 http://hdl.handle.net/123456789/9238 en John Wiley & Sons, Inc.
institution Universiti Malaysia Perlis
building UniMAP Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaysia Perlis
content_source UniMAP Library Digital Repository
url_provider http://dspace.unimap.edu.my/
language English
topic esterification
lauric acid
geraniol
lipozyme
spellingShingle esterification
lauric acid
geraniol
lipozyme
Vazquez-Lima, F.
Pyle, D. L.
Asenjo, J.A.
Factors affecting the esterification of lauric acid using an immobilized biocatalyst: enzyme characterization and studies in a well-mixed reactor
description The esterification of lauric acid with geraniol catalyzed by the commercially immobilized lipase preparation from Mucor miehei, Lipozyme(®), was studied in well-stirred flasks. The enzyme support was characterized in terms of its internal and external surface area, protein location, and protein content. It was found that the enzyme was mainly located on the external surface of the support, therefore, internal diffusional limitations were not important. It was also shown that the protein content of the support depends on the size of the particle, with smaller particles containing higher amounts of protein per unit weight. Under the conditions studied, the reaction was not under external mass transfer limitations, and the initial reaction rate depended on the size of the support particles. This was mainly due to the different protein contents on the support as a function of particle size and not to internal or external mass transfer limitations. Also, it was found that the inhibition exerted by water was predominantly a physical effect due to its accumulation around the enzyme. It was also found that the reaction was substrate inhibited by lauric acid, but not by geraniol. The esterification of lauric acid with geraniol catalyzed by the commercially immobilized lipase preparation from Mucor miehei, Lipozyme, was studied in well-stirred flasks. The enzyme support was characterized in terms of its internal and external surface area, protein location, and protein content. It was found that the enzyme was mainly located on the external surface of the support, therefore, internal diffusional limitations were not important. It was also shown that the protein content of the support depends on the size of the particle, with smaller particles containing higher amounts of protein per unit weight. Under the conditions studied, the reaction was not under external mass transfer limitations, and the initial reaction rate depended on the size of the support particles. This was mainly due to the different protein contents on the support as a function of particle size and not to internal or external mass transfer limitations. Also, it was found that the inhibition exerted by water was predominantly a physical effect due to its accumulation around the enzyme. It was also found that the reaction was substrate inhibited by lauric acid, but not by geraniol.
format Article
author Vazquez-Lima, F.
Pyle, D. L.
Asenjo, J.A.
author_facet Vazquez-Lima, F.
Pyle, D. L.
Asenjo, J.A.
author_sort Vazquez-Lima, F.
title Factors affecting the esterification of lauric acid using an immobilized biocatalyst: enzyme characterization and studies in a well-mixed reactor
title_short Factors affecting the esterification of lauric acid using an immobilized biocatalyst: enzyme characterization and studies in a well-mixed reactor
title_full Factors affecting the esterification of lauric acid using an immobilized biocatalyst: enzyme characterization and studies in a well-mixed reactor
title_fullStr Factors affecting the esterification of lauric acid using an immobilized biocatalyst: enzyme characterization and studies in a well-mixed reactor
title_full_unstemmed Factors affecting the esterification of lauric acid using an immobilized biocatalyst: enzyme characterization and studies in a well-mixed reactor
title_sort factors affecting the esterification of lauric acid using an immobilized biocatalyst: enzyme characterization and studies in a well-mixed reactor
publisher John Wiley & Sons, Inc.
publishDate 2010
url http://dspace.unimap.edu.my/xmlui/handle/123456789/9238
_version_ 1643787833410846720
score 13.22586

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