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Molecules 2014, 19(6), 7629-7645; doi:10.3390/molecules19067629

Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases

1
Departamento de Biocatalisis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain
2
Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga 680001, Colombia
3
Biotransformation and Bioactive Molecules Group, Instituto de Química Avanzada de Cataluña-CSIC Jordi Girona 18-26, 08034 Barcelona, Spain
4
Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455-760 Fortaleza, CE, Brazil
5
Biotechnology, Bioprocess and Biocatalysis Group, Institute of Food Science and Technology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, P.O. Box 15090, ZC 91501-970, Porto Alegre, RS, Brazil
*
Author to whom correspondence should be addressed.
Received: 3 April 2014 / Revised: 3 June 2014 / Accepted: 4 June 2014 / Published: 10 June 2014
(This article belongs to the Special Issue Enzyme Immobilization)
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Abstract

A commercial and very hydrophobic styrene-divinylbenzene matrix, MCI GEL® CHP20P, has been compared to octyl-Sepharose® beads as support to immobilize three different enzymes: lipases from Thermomyces lanuginosus (TLL) and from Rhizomucor miehie (RML) and Lecitase® Ultra, a commercial artificial phospholipase. The immobilization mechanism on both supports was similar: interfacial activation of the enzymes versus the hydrophobic surface of the supports. Immobilization rate and loading capacity is much higher using MCI GEL® CHP20P compared to octyl-Sepharose® (87.2 mg protein/g of support using TLL, 310 mg/g using RML and 180 mg/g using Lecitase® Ultra). The thermal stability of all new preparations is much lower than that of the standard octyl-Sepharose® immobilized preparations, while the opposite occurs when the inactivations were performed in the presence of organic co-solvents. Regarding the hydrolytic activities, the results were strongly dependent on the substrate and pH of measurement. Octyl-Sepharose® immobilized enzymes were more active versus p-NPB than the enzymes immobilized on MCI GEL® CHP20P, while RML became 700-fold less active versus methyl phenylacetate. Thus, the immobilization of a lipase on this matrix needs to be empirically evaluated, since it may present very positive effects in some cases while in other cases it may have very negative ones. View Full-Text
Keywords: lipase immobilization, modulation of lipase activity, interfacial activation, styrene divinylbencene matrix lipase immobilization, modulation of lipase activity, interfacial activation, styrene divinylbencene matrix
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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Garcia-Galan, C.; Barbosa, O.; Hernandez, K.; Santos, J.C.S.; Rodrigues, R.C.; Fernandez-Lafuente, R. Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases. Molecules 2014, 19, 7629-7645.

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