title: Evaluation of styrene-divinylbenzene beads as a support to immobilize lipases.
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.
authors.affiliation: Departamento de Biocatalisis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain. c.garcia@icp.csic.es.
authors.forename: Cristina
authors.initials: C
authors.lastname: Garcia-Galan
authors.affiliation: Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga 680001, Colombia. oveimar@gmail.com.
authors.forename: Oveimar
authors.initials: O
authors.lastname: Barbosa
authors.affiliation: Biotransformation and Bioactive Molecules Group, Instituto de Química Avanzada de Cataluña-CSIC Jordi Girona 18-26, 08034 Barcelona, Spain. khs27883@gmail.com.
authors.forename: Karel
authors.initials: K
authors.lastname: Hernandez
authors.affiliation: Departamento de Biocatalisis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain. jscleiton@gmail.com.
authors.forename: Jose C S
authors.initials: JC
authors.lastname: dos Santos
authors.affiliation: 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. rafaelcrodrigues@ufrgs.br.
authors.forename: Rafael C
authors.initials: RC
authors.lastname: Rodrigues
authors.affiliation: Departamento de Biocatalisis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain. rfl@icp.csic.es.
authors.forename: Roberto
authors.initials: R
authors.lastname: Fernandez-Lafuente
mesh_terms: D004800:Enzymes, Immobilized / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry*; D020058:Styrene / Q000737:chemistry*
chemical_list: D004800:Enzymes, Immobilized; D020058:Styrene; D008049:Lipase