Versatility of glutaraldehyde to immobilize of lipase B from Candida Antarctica- Effect of the immobilization protocol on biocatalytic properties

• Main Authors: Barbosa, Oveimar, Rueda, Nazzoly, Torres Sáez, Rodrigo, Ortiz, Claudia, Fernández-Lafuente, Roberto
• Other Authors: Ministerio de Economía y Competitividad (España)
• Format: Still Image
• Language: unknown
• Published: 2014
• Subjects: Glutaraldehyde; Conformational engineering; Lipase immobilization; Uis; Antarc*; Antarctica
• Online Access: http://hdl.handle.net/10261/189418; https://doi.org/10.13039/501100003329

Trabajo presentado en el VII Workshop on Biocatalysis and Biotransformations - 1º Simposio Latinoamericano de Biocatalisis y Biotransformaciones, celebrado en Búzios (Brasil) del 23 al 26 de septiembre de 2014. [Introduction]: Lipases are enzymes which have a high affinity for hydrophobic surfaces. This is a consequence of the catalytic mechanism of lipases, designed to act in the interface of oil drops, and exhibited the so-called interfacial activation. This work shows how the immobilization of lipases using glutaraldehyde chemistry allows a high versatility, being possible to control the driving force of the immobilization by controlling the experimental conditions: direct covalent attachment using salt and a detergent, ionic exchange using a nonionic detergent and interfacial activation using salt. [Results and discussion]: These different protocols have permitted immobilizing the CALB at different rates, and also to have CALB preparations with quite different properties, mainly when used versus complex substrates. The table 1 shows the specific activities of the different immobilized enzymes, compared to that of the soluble enzyme and the enzyme immobilized in octyl agarose. Considering the sensibility of lipases to the immobilization conditions, differences can be not only attributed to different orientations of the enzyme on the support; the effects of the immobilization medium could also contribute to the observed differences. These differences become very significant studying activity and enantioselectivity of the immobilized enzymes versus R/S methyl mandelate, where the values and their dependence on the experimental conditions are completely different. [Conclusion]: A controlled immobilization of CALB using glutaraldehyde chemistry may contribute to obtaining at least, five different catalysts with very different properties and response to changes in the reaction conditions. This work was supported by grant CTQ2009- 07568 from Spanish Government and VIE-UIS Research Program. Peer Reviewed