Abstract
By radical-catalyzed addition to residual vinyl groups, cysteine was S-linked to porous beads of divinylbenzene/ethylstyrene copolymer. Subsequent treatment with acetic anhydride gave polystyrene-supported azlactone groups able to covalently bind enzymes out of aqueous solution under mild conditions. Pseudomonas cepacia lipase thus immobilized remained active for the hydrolysis of esters, even after storage and/or several cycles of use and recovery.
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Stranix, B.R., Darling, G.D. Functional polymers from (vinyl)polystyrene. Enzyme immobilization through a cysteinyl-S-ethyl spacer. Biotechnol Tech 9, 75–80 (1995). https://doi.org/10.1007/BF00224401
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DOI: https://doi.org/10.1007/BF00224401