Immobilized enzymes have good stability and reusability compared to free enzymes and can be used for rapid screening of enzyme inhibitors.In this study, a novel immobilized α-glucosidase 3-MPBA/AG@aZIF-7/PDA was synthesized and characterized.In addition, Ile-Tyr-Gly (ITG, non-competitive inhibitory peptide) and Cys-Tyr-Gly (CTG, competitive inhibitory peptide) were used as adsorption models to study the adsorption properties of 3-MPBA/AG@aZIF-7/PDA.Results showed that the adsorption capacity of 3-MPBA/AG@aZIF-7/PDA for ITG and CTG was 191.06 mg/g and 129.50 mg/g, respectively, under the optimized adsorption conditions.The adsorption kinetics and adsorption isotherm studies indicated that the adsorption of both ITG and CTG by 3-MPBA/AG@aZIF-7/PDA conformed to the proposed one-stage adsorption kinetic model, which was mainly a physical adsorption process, and the adsorption process conformed to the Langmuir isothermal adsorption model that was dominated by the adsorption of monomolecular layers.Moreover, it was found that the immobilized enzyme could efficiently isolate the AG inhibitory peptides from the complex system.These results indicate that the immobilized enzyme is of great value in isolation and enrichment of functional peptides, and 3-MPBA/AG@aZIF-7/PDA is a promising material for the efficient isolation of α-glucosidase inhibitors.
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