Citation: YUAN Jing-Xiang, WANG Chao-Zhan, WEI Yin-Mao. High-Capacity Strong Cation Exchange Resin Based on Reutilization of An Inactivated Immobilized Enzyme and Its Adsorption Properties for Lysozyme[J]. Chinese Journal of Analytical Chemistry, ;2016, 44(12): 1892-1899. doi: 10.11895/j.issn.0253-3820.160296
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A new cation exchange resin was prepared based on surface-initiated atom transfer radical polymerization (SI-ATRP) of poly (sodium 4-styrene sulfonate) (PNASS) at 30℃ for 3 h from inactivated immobilized enzymes. The cation exchange resin was characterized by Fourier transform infrared spectrometry (FT-IR). Lysozyme was selected as a model protein to evaluate the adsorption performance of the as-prepared cation exchange resin. The effects of protein concentration, ionic strength, organic solvent, contacting time and temperature on protein adsorption were investigated. The results showed that the cation exchange resin exhibited very good performance for the adsorption of lysozyme with a high capacity (240 mg/g) at room temperature and fast speed (within 30 min), which were much better than those reported in previously reported works. The adsorption isotherms could be better fitted by Langmuir model than Freundlich model and the adsorption process followed the pseudo-second-order kinetic model.
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