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Evaluation of styrene-divinylbenzene beads as a support to immobilize lipases

Autores:Cristina Garcia-Galan, José Cleiton Sousa dos Santos, Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Cristina Garcia-Galan 1 , Oveimar Barbosa 2 , Karel Hernandez 3 , Jose C. S. dos Santos  1,4 , Rafael C. Rodrigues 5, Roberto Fernandez-Lafuente 1*
1    Departamento de Biocatalisis. ICP-CSIC. Campus UAM-CSIC. Cantoblanco. 28049 Madrid. Spain; E-Mail: c.garcia@icp.csic.es
2     Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia; E-Mail: oveimar@gmail.com
3     Biotransformation and Bioactive Molecules Group. Instituto de Química Avanzada de Cataluña-CSIC Jordi Girona 18-26, 08034. Barcelona (Spain); E-Mail: khs27883@gmail.com
4     Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455-760, Fortaleza, CE, Brazil; E-Mail: jscleiton@gmail.com
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; E-Mail: rafaelcrodrigues@ufrgs.br

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.
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