Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase
| Author | Daryoush Abedi | en |
| Author | Mohammad Reza Fazeli | en |
| Author | Abbas Jafarian | en |
| Issued Date | 2004-07-31 | en |
| Abstract | Penicillin G acylase from E. coli TA1 was immobilized by Cross-Linked Enzyme Aggregates (CLEA), a new method for immobilization. This biocatalyst and commercial immobilized penicillin G acylase (PGA-450) were used to study the effect of pH, temperature and substrate concentration on the synthesis of ampicillin from phenyl glycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA). Compared with PGA-450, this immobilized enzyme showed a high synthesis activity. The optimum conditions for synthetic activity was at pH 6, 25°C and 2:6 (6-APA:PGME) substrate ratio. | en |
| DOI | https://doi.org/10.22037/ijpr.2010.594 | en |
| Keyword | E. coli | en |
| Keyword | Penicillin G acylase | en |
| Keyword | Cross-linked Enzyme Aggregates | en |
| Keyword | Ampicillin | en |
| Publisher | Brieflands | en |
| Title | Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase | en |
| Type | Research Article | en |
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