Enzyme activation for nonaqueous media
β Scribed by Moo-Yeal Lee; Jonathan S Dordick
- Book ID
- 108476136
- Publisher
- Elsevier Science
- Year
- 2002
- Tongue
- English
- Weight
- 129 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0958-1669
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The catalytic activities of lyophilized powders of β£-chymotrypsin and Candida antarctica lipase were found to increase 4-to 8-fold with increasing amounts of either buffer salts or potassium chloride in the enzyme preparation. Increasing amounts of sorbitol in the chymotrypsin preparation produced a
## Abstract A protein solubilization method has been developed to directly solubilize protein clusters into organic solvents containing small quantities of surfactant and trace amounts of water. Termed βdirect solubilization,β this technique was shown to solubilize three distinct proteinsβsubtilisi
The rates of transesterification reactions catalyzed by the protease subtilisin Carlsberg suspended in various anhydrous solvents at 30Β°C can be increased more than 100fold by the addition of denaturing organic cosolvents (dimethyl sulfoxide or formamidef; in water, the same cosolvents exert no enzy
We have investigated features for minimizing the inactivation of tyrosinase (E.C. 1.14.18.1) that is caused by immobilization on glass beads and Celite@. The degree of inactivation is dependent on the enzyme loading and the carrier's surface area. Addition of a sacrificial protein during the immobil