## Abstract Penicillin V acylase from the actinomycete __Streptomyces lavendulae__ ATCC 13664 has been immobilized to epoxy‐activated acrylic beads (Eupergit C®) by covalent binding. Further linkage of bovine serum albumin after enzyme immobilization was carried out in order to remove the remaining
Enhanced production of penicillin V acylase fromStreptomyces lavendulae
✍ Scribed by R. Torres; F. Ramón; I. de la Mata; C. Acebal; M. P. Castillón
- Book ID
- 105954763
- Publisher
- Springer
- Year
- 1999
- Tongue
- English
- Weight
- 124 KB
- Volume
- 53
- Category
- Article
- ISSN
- 1432-0614
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Penicillin V acylase from jFusarium sp. SKF 235 was i~obilized on several cation-exchange resins, of which Amberlite CG-50 was preferred. Maximum activity of the immobilized penicillin V acylase was 250 to 280 W/g dry beads. The pH and temperature optima of the enzyme shifted from 6.5 to 6.8 a
Escherichia coli cells with penicillin acylase activity were permeabilized with aqueous solutions of the cationic detergent N-cetyl-N,N,N-trimethylammonium bromide (CTAB), at pH 8.0 and the activity was found to have almost doubled. The concentration of CTAB, the time and temperature of treatment we