Abstract
Whereas the beta-lactam acylases are traditionally used for the hydrolytic processing of penicillin G and cephalosporin C, new and mutated acylases can be used for the hydrolysis of alternative fermentation products as well as for the synthesis of semisynthetic beta-lactam antibiotics. Three-dimensional structural analyses and site-directed mutagenesis studies have increased the understanding of the catalytic mechanism of these enzymes. The yield of hydrolysis and synthesis has been greatly improved by process design, including immobilization of the enzyme and the use of alternative reaction media. Significant advances have also been made in the resolution of racemic mixtures by means of stereoselective acylation/hydrolysis using beta-lactam acylases
| Original language | English |
|---|---|
| Pages (from-to) | 349-355 |
| Number of pages | 7 |
| Journal | Current Opinion in Biotechnology |
| Volume | 15 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 2004 |
Keywords
- PENICILLIN-G ACYLASE
- ACID ESTER HYDROLASE
- SITE-DIRECTED MUTAGENESIS
- N-TERMINAL HYDROLASE
- SUBSTRATE-SPECIFICITY
- CEPHALOSPORIN ACYLASE
- ENZYMATIC-SYNTHESIS
- 7-AMINOCEPHALOSPORANIC ACID
- AUTOPROTEOLYTIC ACTIVATION
- ACETOBACTER-TURBIDANS