Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6482211 | Biochemical Engineering Journal | 2018 | 7 Pages |
Abstract
This work reports poly(allylamine) of 900â¯kDa (PAA-L) as a polymeric ligand for protein ion-exchange chromatography. PAA-L-modified Sepharose FF with 9 ionic capacities (ICs) from 80 to 880â¯mmol/L were prepared and bovine serum albumin adsorption and chromatography were investigated. With increasing IC, protein adsorption capacity increased somewhat in the IC range of 80-420â¯mmol/L, and then increased twice in the IC range of 420-740â¯mmol/L, and finally kept unchanged till 880â¯mmol/L; the uptake rate (De/D0) increased about 14 times (from 0.029 to 0.42) in the IC range of 420-700â¯mmol/L, and finally kept almost unchanged till 880â¯mmol/L. The maximum adsorption capacity and uptake rate of the resins reached 336â¯mg/mL and 0.42, which were 24% and 2.5 times respectively larger than those of 17.5â¯kDa PAA-grafted resins. The selected PAA-L resin of ICâ¯=â¯740â¯mmol/L was salt-tolerant up to 750â¯mmol/L NaCl. The dynamic binding capacity (DBC) of this resin showed a maximum of 142â¯mg/mL at 350â¯mmol/L NaCl, and kept over 90â¯mg/mL in the range of 150-500â¯mmol/L NaCl. Linear gradient elution on the column of this resin proved high protein recovery (>97%) and stability of the column. Taken together, the results indicate that the PAA-L resin was a promising anion exchanger for high-performance protein chromatography for use at extended ionic strengths.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Ming Li, Linling Yu, Yang Liu, Yan Sun,