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.
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http://dx.doi.org/10.1007/978-1-0716-0215-7_7 | DOI Listing |
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