Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase
| Autor: | João Carlos Marcos, Joaquim M. S. Cabral, Xing-yan Wu, Xuejun Cao, Luís P. Fonseca |
|---|---|
| Přispěvatelé: | Universidade do Minho |
| Rok vydání: | 2004 |
| Předmět: |
Bioconversion
0106 biological sciences Penicillin acylase Penicillanic Acid Bioengineering Penicillin amidase medicine.disease_cause 01 natural sciences 7. Clean energy Applied Microbiology and Biotechnology Catalysis 010608 biotechnology PEG ratio medicine Escherichia coli Science & Technology Chromatography Aqueous solution 010405 organic chemistry Chemistry Temperature Substrate (chemistry) Penicillin G Recombinant E. coli A56 General Medicine Hydrogen-Ion Concentration Recombinant Proteins 0104 chemical sciences 3. Good health Penicillin Biochemistry Aqueous two-phase systems Penicillin Amidase 6-aminopenicillanic acid production Crystallization Biotechnology medicine.drug |
| Zdroj: | Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP |
| ISSN: | 0141-5492 |
| Popis: | Bioconversion of Penicillin G in PEG 20000-Dextran T 70 aqueous two-phase systems was achieved using the recombinant Escherichia coli A56 (ppA22) with intracellular penicillin acylase as catalyst. The best conversion conditions were attained for: 7%(w/v) substrate (penicillin G), enzyme activity in bottom phase 52 U/ml, pH 7.8, temperature 37°C, reaction time 40 min. Five repeated batches could be performed in these conditions. Conversions ratios between 0.902-0.985mol of 6-aminopenicillanic acid (6-APA) per mol of penicillin G, were obtained and specific productivity was 3.6-4.6 μmol/min•ml. In addition the product 6-APA could directly be crystallized from the top phase with a purity of 96.2%. Science & Technological Commission of Shanghai Municipal People’s Government. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink