Enzymes covalently bound to acrylic gel beads. I. Interaction of hydrophilic anionic gel beads with biomacromolecules

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Abstract
Gel beads of excellent mechanical properties are obtained by copolymerization of methacrylic acid anhydride with acrylamide using ethyleneglycoldimethacrylate or N, N′‐methylene‐bis (methacrylamide) as a cross‐linker.When protein is covalently bound to the anhydride groups of the beads, residual anhydride groups are hydrolyzed to form an anionic matrix (AM). The hydrophilic gel beads are stable to 1M NaOH, mechanical stirring, and dehydration by lyophilization or organic solvents. Proteases, nucleases, and amylases bound to AM are efficient catalysts in breaking down high molecular weight substrates.As far as the interaction of AM with biomacromolecules at pH 7.5 in 0.05M phosphate buffer is concerned, polyanions like DNA or tRNA are strictly excluded from the gel volume, whereas cationic polymers like basic proteins are strongly absorbed even at an ionic strength of 0.3. Little or no interaction is observed with neutral biopolymers.