Enhancing protein capacity of rigid macroporous polymeric adsorbent

Biotechnol Prog. 2001 Nov-Dec;17(6):1093-8. doi: 10.1021/bp010108y.

Abstract

A macroporous poly(glycidyl methacrylate-triallyl isocyanurate-divinylbenzene) resin was synthesized and modified with diethylamine to yield an anion-exchange resin suitable for protein adsorption. Efforts were made to enhance protein ion exchange capacity of the resin by investigating the copolymer composition. Different synthesis recipes were attempted, and the resultant resins were characterized by measuring the specific surface area and the adsorption ability using bovine serum albumin (BSA) as a model protein. The intraparticle pore size distribution measured by mercury porosimetry showed that the pores in the range of 40-120 nm took 75% of the total pore volume, indicating that the ion exchanger was favorable for protein adsorption. BSA capacity obtained with an appropriate recipe was as high as 78.6 mg/g wet resin or 50 mg/mL packed volume, which was higher than the capacities of some commercially available ion exchangers. Moreover, by using a pore diffusion model, the effective pore diffusivity of BSA was found to be 5.5 x 10(-12) m(2)/s, similar to those in the commercial ion exchangers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Algorithms
  • Chemical Phenomena
  • Chemistry, Physical
  • Chromatography, Ion Exchange
  • Cross-Linking Reagents
  • Ion Exchange Resins / chemistry*
  • Polymers
  • Polymethacrylic Acids / chemistry*
  • Polyvinyls / chemistry*
  • Porosity
  • Proteins / chemistry*
  • Serum Albumin, Bovine / chemistry
  • Solvents

Substances

  • Cross-Linking Reagents
  • Ion Exchange Resins
  • Polymers
  • Polymethacrylic Acids
  • Polyvinyls
  • Proteins
  • Solvents
  • poly(glycidyl methacrylate-triallyl isocyanurate-divinylbenzene)
  • Serum Albumin, Bovine