Abstract：
:Two different approaches of matrix assisted refolding have been evaluated and compared to conventional refolding by dilution. Bovine alpha-lactalbumin was used for the studies as model protein. It was adsorbed under denaturing conditions on an ion exchange matrix and refolding was completed on the column prior to elution or, depending on the buffer system, in the eluate. Agarose based chromatography matrices showed high capacities for the denatured alpha-lactalbumin. A positive effect on the yield of refolded protein by the matrix could be observed for Fractogel EMD DEAE and a negative for Toyopearl DEAE 650M, DEAE Sepharose FF and Q Sepharose FF. In the case of Fractogel EMD DEAE the ion exchange surface might act as a folding helper. This property may be caused by the grafted polymers. For Source 30Q only a marginal negative influence on the refolding kinetics was observed, thus the ion exchanger is only a mean for removal of chaotropic agents. Refolding on the column is characterized by a low yield but high productivity due to significant reduction of refolding time.
journal_name
J Biotechnoljournal_title
Journal of biotechnologyauthors
Machold C,Schlegl R,Buchinger W,Jungbauer Adoi
10.1016/j.jbiotec.2005.01.004subject
Has Abstractpub_date
2005-04-20 00:00:00pages
83-97issue
1eissn
0168-1656issn
1873-4863pii
S0168-1656(05)00030-1journal_volume
117pub_type
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