Advanced

Superporous agarose beads as a hydrophobic interaction chromatography support

Gustavsson, Per-Erik LU ; Axelsson, Anders LU and Larsson, Per-Olof LU (1999) In Journal of Chromatography A 830(2). p.275-284
Abstract
Superporous agarose beads were used as a support for hydrophobic interaction chromatography. These beads have large connecting flow pores in addition to their normal diffusion pores. The flow pores, which are approximately one fifth of the overall diameter of the superporous agarose beads, were earlier shown to give the beads improved mass transfer properties relative to homogeneous agarose beads (Gustavsson and Larsson, J. Chromatogr. A, 734 (1996) 231-240). Superporous agarose beads and homogeneous agarose beads of the same particle size range (106-180 mu m) were derivatized with phenyl groups. The properties of the superporous beads were then compared with the homogeneous beads in the separation of a mixture of three model proteins... (More)
Superporous agarose beads were used as a support for hydrophobic interaction chromatography. These beads have large connecting flow pores in addition to their normal diffusion pores. The flow pores, which are approximately one fifth of the overall diameter of the superporous agarose beads, were earlier shown to give the beads improved mass transfer properties relative to homogeneous agarose beads (Gustavsson and Larsson, J. Chromatogr. A, 734 (1996) 231-240). Superporous agarose beads and homogeneous agarose beads of the same particle size range (106-180 mu m) were derivatized with phenyl groups. The properties of the superporous beads were then compared with the homogeneous beads in the separation of a mixture of three model proteins (ribonuclease A, lysozyme and bovine serum albumin) at various superficial flow velocities from 30 to 600 cm/h. The superporous beads gave satisfactory separation at flow velocities five times higher than was possible for homogeneous beads. The performance of the two types of beads was also compared in the purification of lactate dehydrogenase from a beef heart extract at a superficial flow velocity of 150 cm/h. The superporous beads performed considerably better, leading to twice the purification factor and twice the concentration of the desired product. The results were interpreted using the theoretical treatment given by Carta and Rodrigues (Carta and Rodrigues, Chem. Eng. Sci., 48 (1993) 3927). (C) 1999 Elsevier Science B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
stationary phases, LC, flow pores, agarose, superporous, ribonuclease A, lysozyme, bovine serum albumin
in
Journal of Chromatography A
volume
830
issue
2
pages
275 - 284
publisher
Elsevier
external identifiers
  • wos:000078328400003
  • scopus:0032927212
ISSN
0021-9673
DOI
10.1016/S0021-9673(98)00899-1
language
English
LU publication?
yes
id
0e6faedf-fe98-499c-aa85-327202845425 (old id 3917224)
date added to LUP
2013-07-03 12:37:46
date last changed
2017-01-01 07:13:46
@article{0e6faedf-fe98-499c-aa85-327202845425,
  abstract     = {Superporous agarose beads were used as a support for hydrophobic interaction chromatography. These beads have large connecting flow pores in addition to their normal diffusion pores. The flow pores, which are approximately one fifth of the overall diameter of the superporous agarose beads, were earlier shown to give the beads improved mass transfer properties relative to homogeneous agarose beads (Gustavsson and Larsson, J. Chromatogr. A, 734 (1996) 231-240). Superporous agarose beads and homogeneous agarose beads of the same particle size range (106-180 mu m) were derivatized with phenyl groups. The properties of the superporous beads were then compared with the homogeneous beads in the separation of a mixture of three model proteins (ribonuclease A, lysozyme and bovine serum albumin) at various superficial flow velocities from 30 to 600 cm/h. The superporous beads gave satisfactory separation at flow velocities five times higher than was possible for homogeneous beads. The performance of the two types of beads was also compared in the purification of lactate dehydrogenase from a beef heart extract at a superficial flow velocity of 150 cm/h. The superporous beads performed considerably better, leading to twice the purification factor and twice the concentration of the desired product. The results were interpreted using the theoretical treatment given by Carta and Rodrigues (Carta and Rodrigues, Chem. Eng. Sci., 48 (1993) 3927). (C) 1999 Elsevier Science B.V. All rights reserved.},
  author       = {Gustavsson, Per-Erik and Axelsson, Anders and Larsson, Per-Olof},
  issn         = {0021-9673},
  keyword      = {stationary phases,LC,flow pores,agarose,superporous,ribonuclease A,lysozyme,bovine serum albumin},
  language     = {eng},
  number       = {2},
  pages        = {275--284},
  publisher    = {Elsevier},
  series       = {Journal of Chromatography A},
  title        = {Superporous agarose beads as a hydrophobic interaction chromatography support},
  url          = {http://dx.doi.org/10.1016/S0021-9673(98)00899-1},
  volume       = {830},
  year         = {1999},
}