Control of enzyme activity in stirred bioreactors
- 28 February 1993
- journal article
- Published by Elsevier in The Chemical Engineering Journal
- Vol. 51 (1) , B11-B16
- https://doi.org/10.1016/0300-9467(93)80010-l
Abstract
No abstract availableKeywords
This publication has 8 references indexed in Scilit:
- Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transitionBiochemistry, 1991
- Intermediates in guanidine-HCl unfolding of glutamine synthetase from the extreme thermophile, Bacillus caldolyticusBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Correlation of enzymatic activities and aggregation state in chicken liver fatty acid synthaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Synergistic ligand protection and intermediates in the denaturation of extremely thermophilic glutamine synthetaseBiochemistry, 1987
- Unfolding and refolding of a type .kappa. immunoglobulin light chain and its variable and constant fragmentsBiochemistry, 1987
- Enzyme stabilization towards thermal, chemical and proteolytic deactivationEnzyme and Microbial Technology, 1985
- Unfolding-refolding transition of a hinge bending enzyme: horse muscle phosphoglycerate kinase induced by guanidine hydrochlorideBiochemistry, 1984
- A mathematical analysis of enzyme stabilization by a series‐type mechanism: Influence of chemical modifiersBiotechnology & Bioengineering, 1984