Effect of shear on the inactivation kinetics of the enzyme dextransucrase
β Scribed by Robert W. Lencki; Alberto Tecante; Lionel Choplin
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 698 KB
- Volume
- 42
- Category
- Article
- ISSN
- 0006-3592
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π SIMILAR VOLUMES
## Abstract Enzyme inactivation kinetics typically follows what would appear to be simple firstβorder behavior. However, the inactivation process is known to involve a number of reversible (decomposition, denaturation) as well as irreversible (decomposition, aggregation, and coagulation) reactions.
Evidence is presented to show that the presence of a channelled reaction branch in a coupled two-enzyme reaction leads to a slower overall relaxation of the system towards steady state following perturbations of the reaction conditions. A predominant part of the total reaction flux change resulting