Are you interested in covalent attachment of the enzyme to the support, or electrostatic immobilization? Anion exchange resins with functionality such as DEAE and QAE are used in protein purification because proteins bind to them electrostatically and can be eluted by increasing the ionic strength of the medium.
Enzymes can be covalently attached to primary-amine containing supports by crosslinking to carboxylate side chains (aspartate, glutamate) using carbodiimide crosslinkers, or by crosslinking to amino side chains (lysine) using amine-to-amine crosslinkers.
Thanks a lot Adam for the informative answer, I am thinking about synthesizing a simple polymer with free amino groups to use them as supports for different types of enzyme, I tend to the covenant bonding because I think it is more stable to be reusable! am I right?!
Common practice is to use Glutaraldehyde as a coupling agent between the amine of the polymer support to the protein. Although this would enable covalent binding and better reusability; most of the times upon crosslinking, enzymes tend to lose activity. I recommend epoxide functionality.