Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase
| Main Author: | |
|---|---|
| Publication Date: | 2004 |
| Other Authors: | , , , |
| Format: | Article |
| Language: | eng |
| Source: | Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
| Download full: | http://hdl.handle.net/1822/1962 |
Summary: | 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%. |
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Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase6-aminopenicillanic acid productionAqueous two-phase systemsBioconversionRecombinant E. coli A56Penicillin acylaseScience & TechnologyBioconversion 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.KluwerUniversidade do MinhoCao, Xue-junWu, Xing-yanFonseca, Luís PinaCabral, J. M. S.Marcos, João Carlos20042004-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/1962eng"Biotechnology letters". 26 (2004) 97-101.0141-549210.1023/B:BILE.0000012885.62462.f315000474info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-05-11T05:30:41Zoai:repositorium.sdum.uminho.pt:1822/1962Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T15:20:52.440928Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse |
| dc.title.none.fl_str_mv |
Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase |
| title |
Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase |
| spellingShingle |
Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase Cao, Xue-jun 6-aminopenicillanic acid production Aqueous two-phase systems Bioconversion Recombinant E. coli A56 Penicillin acylase Science & Technology |
| title_short |
Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase |
| title_full |
Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase |
| title_fullStr |
Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase |
| title_full_unstemmed |
Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase |
| title_sort |
Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase |
| author |
Cao, Xue-jun |
| author_facet |
Cao, Xue-jun Wu, Xing-yan Fonseca, Luís Pina Cabral, J. M. S. Marcos, João Carlos |
| author_role |
author |
| author2 |
Wu, Xing-yan Fonseca, Luís Pina Cabral, J. M. S. Marcos, João Carlos |
| author2_role |
author author author author |
| dc.contributor.none.fl_str_mv |
Universidade do Minho |
| dc.contributor.author.fl_str_mv |
Cao, Xue-jun Wu, Xing-yan Fonseca, Luís Pina Cabral, J. M. S. Marcos, João Carlos |
| dc.subject.por.fl_str_mv |
6-aminopenicillanic acid production Aqueous two-phase systems Bioconversion Recombinant E. coli A56 Penicillin acylase Science & Technology |
| topic |
6-aminopenicillanic acid production Aqueous two-phase systems Bioconversion Recombinant E. coli A56 Penicillin acylase Science & Technology |
| description |
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%. |
| publishDate |
2004 |
| dc.date.none.fl_str_mv |
2004 2004-01-01T00:00:00Z |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
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article |
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publishedVersion |
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http://hdl.handle.net/1822/1962 |
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http://hdl.handle.net/1822/1962 |
| dc.language.iso.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
"Biotechnology letters". 26 (2004) 97-101. 0141-5492 10.1023/B:BILE.0000012885.62462.f3 15000474 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
| dc.publisher.none.fl_str_mv |
Kluwer |
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Kluwer |
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info@rcaap.pt |
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