Abstract
Protein-imprinted polyacrylamide gel beads (IPGB) were synthesized via inverse suspension polymerization, using staphylococcal enterotoxin B (SEB) as template. The adsorption capacity of SEB-IPGB was almost three times as much as that of non-imprinted gel beads. The Langmuir adsorption models were applied to describe the equilibrium isotherms. The results showed that an equal class of adsorption was formed in the SEB-IPGB with the maximum adsorption capacity of 8.40 mg SEB/g imprinted beads. The selectivity test of imprinted beads shows that they exhibited good recognition for SEB as compared with the other proteins. The formation of multiple hydrogen bonds and complementary shape between the imprinting cavities and the template proteins would be the two factors that led to the imprinting effect. The obtained SEB-IPGB would be used as a potential material for protein toxin separation, extraction, and purification. Copyright © 2014 John Wiley & Sons, Ltd.
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