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Preparation and adsorption behavior of a cellulose‐based,mixed‐mode adsorbent with a benzylamine ligand for expanded bed applications
Authors:Dong Gao  Shan‐Jing Yao  Dong‐Qiang Lin
Affiliation:1. Department of Chemical and Biochemical Engineering, Zhejiang University, Hangzhou 310027, China;2. Institute of Modern Separation Science, Key Laboratory of Separation Science in Shaanxi Province, Northwest University, Xi'an 710069, China
Abstract:A novel mixed‐mode expanded bed adsorbent with anion‐exchange properties was explored with benzylamine as the functional ligand. The cellulose composite matrix, densified with stainless steel powder, was prepared with the method of water‐in‐oil suspension thermal regeneration. High activation levels of the cellulose matrix were obtained with allyl bromide because of the relative inertness of the allyl group under the conditions of the activation reaction. After the formation of the bromohydrin with N‐bromosuccinimide and coupling with benzylamine, the activated matrix was derived to function as a mixed‐mode adsorbent containing both hydrophobic and ionic groups. The protein adsorption capacity was investigated with bovine serum albumin as a model protein. The results indicated that the prepared adsorbent could bind bovine serum albumin with a high adsorption capacity, and it showed salt tolerance. Effective desorption was achieved by a pH adjustment across the isoelectric point of the protein. The interactions between the cell and adsorbent were studied, and the bioadhesion was shielded by the adjustment of the salt concentration above 0.1M. Stable fluidization in the expanded bed was obtained even in a 2% (dry weight) yeast suspension. The direct capture of target proteins from a biomass‐containing feedstock without extra dilution steps could be expected with the mixed‐mode adsorbent prepared in this work, and this would be especially appropriate for expanded bed adsorption applications. © 2007 Wiley Periodicals, Inc. J Appl Polym Sci, 2008
Keywords:chromatography  functionalization of polymers  ion exchangers  proteins  separation techniques
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