Characteristics of immobilized invertase
β Scribed by Hiroshi Ooshima; Masuo Sakimoto; Yoshio Harano
- Publisher
- John Wiley and Sons
- Year
- 1981
- Tongue
- English
- Weight
- 32 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Invertase from __Candida utilis__ was immobilized on porous cellulose beads by an ionicβquanidino bond. The immobilized invertase showed optimum activity between pH 4.0 and 5.4, while the free enzyme had a sharp optimum at pH 4.1. Both temperature profiles were fairly similar up to 55Β°C
After periodate oxidation of its glycosidic component, invertase was covalently bound onto three types of modified solid supports: glycidyl methacrylate, styrene-divinylbenzene copolymers, and bead cellulose. Direct reaction of the invertase aldehyde groups that were formed with amino groups of the