Chemical modification of lipase b of candida antarctica in solid phase for improving biochemical properties

Abstract

[Introduction]: Chemical modification of enzymes is a strategy widely used in biocatalysis for design of biocatalysts with improved biochemical properties. when the chemical modification is performed on immobilized enzymes, we can protect the enzyme from side-effects that are normally produced with modification of the soluble form of the enzymes. In this work, we modified CALB through two differentmethodologies, and the effect of these modification on the activity, stability and specificity of the enzyme was studied.

[Results and discussion]: The effect of chemical modification on the enzyme activity of CALB immobilized on octyl-agarose (OC) and Cyanogen Bromide-agarose (BrCN) were evaluated. In Table 1 are shown changes in enzyme activity of CALB by chemical modification produced by modification (100%) with EDA and TNBS.In Table 2 are shown enzyme activity and enantioselectivity of the different derivatives on (R/S)-Methyl mandelate. Modification of lipase caused different activity and enatioselectivity results, demonstrating that both activity and selectivity of lipase are affected depending on the type of enzyme modification.

[Conclusion]: This work exemplifies as chemical modification on solid phase allows modulating biochemical properties of lipases, affecting activity, stability and enantioselectivity of these enzymes.