Immobilization of Enzymes on Supports Activated with Glutaraldehyde: A Very Simple Immobilization Protocol
In this chapter, we describe different approaches for the utilization of glutaraldehyde in protein immobilization. First, we focus on the covalent attachment of proteins to glutaraldehyde-activated matrixes. We describe conditions for the synthesis of such supports and provide an example of the immobilization and stabilization of a fructosyltransferase. We also describe how glutaraldehyde may be used for the cross-linking of protein–protein aggregates and protein adsorbed onto amino-activated matrixes. In these cases, glutaraldehyde bridges either two lysine groups from different protein molecules or a lysine from the protein structure and an amine group from the support. Examples of cross-linking are given for the immobilization of a d-amino acid oxidase on different amino-activated supports.
Key wordsGlutaraldehyde Protein immobilization Cross-linking Protein stabilization
- 9.Betancor L, López-Gallego F, Hidalgo A, Alonso-Morales N, Mateo GD-OC, Fernández-Lafuente R, Guisán JM (2006) Different mechanisms of protein immobilization on glutaraldehyde activated supports: effect of support activation and immobilization conditions. Enzym Microb Technol 39:877–882CrossRefGoogle Scholar