| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6488279 | Enzyme and Microbial Technology | 2015 | 27 Pages |
Abstract
- Lipase immobilization rate on octyl supports is reduced at high ionic strength.
- Octyl-lipase is more rapidly inhibited by D-pNPP than covalent preparations.
- Octyl-lipase inhibition by D-pNPP did not depend on ionic strength.
- Octyl-lipase activity is less depended on ionic strength.
- Lipase activity is not only depended on catalytic Ser exposition.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Evelin A. Manoel, José C.S. dos Santos, Denise M.G. Freire, Nazzoly Rueda, Roberto Fernandez-Lafuente,