The influence of mixing on lysozyme renaturation during refolding in an oscillatory flow and a stirred-tank reactor
- 1 May 2002
- journal article
- Published by Elsevier in Chemical Engineering Science
- Vol. 57 (10) , 1679-1684
- https://doi.org/10.1016/s0009-2509(02)00066-0
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Oxidative Renaturation of Hen Egg-White Lysozyme. Folding vs AggregationBiotechnology Progress, 1998
- Effect of Additives on Refolding of a Denatured ProteinBiotechnology Progress, 1998
- Design analysis for refolding monomeric proteinAIChE Journal, 1997
- Refolding of Denatured and Denatured/Reduced Lysozyme at High ConcentrationsJournal of Biological Chemistry, 1996
- High cell-density culture of Escherichia coliTrends in Biotechnology, 1996
- Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chainsProtein Science, 1995
- Effective renaturation of reduced lysozyme by gentle removal of ureaProtein Engineering, Design and Selection, 1995
- A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozymeBiochemistry, 1991
- Interactions of proteins with solvent components in 8 m ureaArchives of Biochemistry and Biophysics, 1981
- Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregationBiochemistry, 1979