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

Molecules

Cristina Garcia-Galan²  Oveimar Barbosa³  Karel Hernandez⁴  Jose C. S. dos Santos²  Rafael C. Rodrigues¹ 

[1] 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:;Departamento de Biocatalisis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain; E-Mails:;Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga 680001, Colombia; E-Mail:;Biotransformation and Bioactive Molecules Group, Instituto de Química Avanzada de Cataluña-CSIC Jordi Girona 18-26, 08034 Barcelona, Spain; E-Mail:

关键词: lipase immobilization;    modulation of lipase activity;    interfacial activation;    styrene divinylbencene matrix;   

DOI  :  10.3390/molecules19067629

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.