Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase

Bibliographic Details
Main Author: Cao, Xue-jun
Publication Date: 2004
Other Authors: Wu, Xing-yan, Fonseca, Luís Pina, Cabral, J. M. S., Marcos, João Carlos
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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spelling 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
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/1822/1962
url 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
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Kluwer
publisher.none.fl_str_mv Kluwer
dc.source.none.fl_str_mv reponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
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reponame_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
collection Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
repository.name.fl_str_mv Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
repository.mail.fl_str_mv info@rcaap.pt
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