Loughborough University
Leicestershire, UK
LE11 3TU
+44 (0)1509 263171
Loughborough University

Loughborough University Institutional Repository

Please use this identifier to cite or link to this item: https://dspace.lboro.ac.uk/2134/12017

Title: Multi-cycle recovery of lactoferrin and lactoperoxidase from crude whey using fimbriated high-capacity magnetic cation exchangers and a novel "rotor-stator" high-gradient magnetic separator
Authors: Brown, Geoffrey N.
Muller, Christine
Theodosiou, Eirini
Thomas, Owen R.T.
Franzreb, Matthias
Issue Date: 2013
Publisher: © John Wiley & Sons, Inc.
Citation: BROWN, G.N. ... et al, 2013. Multi-cycle recovery of lactoferrin and lactoperoxidase from crude whey using fimbriated high-capacity magnetic cation exchangers and a novel "rotor-stator" high-gradient magnetic separator. Biotechnology and Bioengineering, 110 (6), pp. 1714–1725.
Abstract: Cerium (IV) initiated "graft-from" polymerization reactions were employed to convert M-PVA magnetic particles into polyacrylic acid-fimbriated magnetic cation exchange supports displaying ultra-high binding capacity for basic target proteins. The modifications, which were performed at 25mg and 2.5g scales, delivered maximum binding capacities (Q) for hen egg white lysozyme in excess of 320mgg, combined with sub-micromolar dissociation constants (0.45-0.69μm) and "tightness of binding" values greater than 49Lg. Two batches of polyacrylic acid-fimbriated magnetic cation exchangers were combined to form a 5g pooled batch exhibiting Q values for lysozyme, lactoferrin, and lactoperoxidase of 404, 585, and 685mgg, respectively. These magnetic cation exchangers were subsequently employed together with a newly designed "rotor-stator" type HGMF rig, in five sequential cycles of recovery of lactoferrin and lactoperoxidase from 2L batches of a crude sweet bovine whey feedstock. Lactoferrin purification performance was observed to remain relatively constant from one HGMF cycle to the next over the five operating cycles, with yields between 40% and 49% combined with purification and concentration factors of 37- to 46-fold and 1.3- to 1.6-fold, respectively. The far superior multi-cycle HGMF performance seen here compared to that observed in our earlier studies can be directly attributed to the combined use of improved high capacity adsorbents and superior particle resuspension afforded by the new "rotor-stator" HGMS design. © 2013 Wiley Periodicals, Inc.
Description: This is the peer reviewed version of the following article: BROWN, G.N. ... et al, 2013. Multi-cycle recovery of lactoferrin and lactoperoxidase from crude whey using fimbriated high-capacity magnetic cation exchangers and a novel "rotor-stator" high-gradient magnetic separator. Biotechnology and Bioengineering, 110 (6), pp. 1714–1725, which has been published in final form at http://dx.doi.org/10.1002/bit.24842. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
Version: Accepted for publication
DOI: 10.1002/bit.24842
URI: https://dspace.lboro.ac.uk/2134/12017
Publisher Link: http://dx.doi.org/10.1002/bit.24842
ISSN: 0006-3592
Appears in Collections:Published Articles (Chemical Engineering)

Files associated with this item:

File Description SizeFormat
Multi-cycle recovery of Lactoferrin and Lactoperoxidase from crude whey using fimbriated high-capacity magnetic cation exchangers and a novel 'roto stator' High Gradient Magnetic Separator.pdfAccepted version567.29 kBAdobe PDFView/Open

 

SFX Query

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.