Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylase

Detalhes bibliográficos
Autor(a) principal: Ferreira,A. L. O.
Data de Publicação: 2004
Outros Autores: Giordano,R. L. C., Giordano,R. C.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Chemical Engineering
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322004000400002
Resumo: An experimental design was applied to improve the reaction conditions for enzymatic synthesis of ampicillin from phenylglycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA), catalyzed by penicillin G acylase from E. coli immobilized on an agarose-glyoxyl derivative. The presence and magnitude of interactions between reaction variables were estimated using a 2(5) factorial design. A batch reactor was employed to assess the influence of the following variables: pH, temperature, initial 6-APA concentration, buffer concentration, and the presence of methanol. Response variables were productivity, selectivity, and yield (based on initial 6-APA concentration). The best synthesis yield (56.9%) was at T = 4ºC and pH 6.5. The highest productivity (49.3 ´ 10-3mM of antibiotic/min) was achieved at T = 25ºC and pH 6.5. Our results indicate that it is possible to achieve high productivity for this system while maintaining a high selectivity and yield.
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spelling Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylaseAmpicillinimmobilized enzymebeta -lactam antibiotic synthesisfactorial designAn experimental design was applied to improve the reaction conditions for enzymatic synthesis of ampicillin from phenylglycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA), catalyzed by penicillin G acylase from E. coli immobilized on an agarose-glyoxyl derivative. The presence and magnitude of interactions between reaction variables were estimated using a 2(5) factorial design. A batch reactor was employed to assess the influence of the following variables: pH, temperature, initial 6-APA concentration, buffer concentration, and the presence of methanol. Response variables were productivity, selectivity, and yield (based on initial 6-APA concentration). The best synthesis yield (56.9%) was at T = 4ºC and pH 6.5. The highest productivity (49.3 ´ 10-3mM of antibiotic/min) was achieved at T = 25ºC and pH 6.5. Our results indicate that it is possible to achieve high productivity for this system while maintaining a high selectivity and yield.Brazilian Society of Chemical Engineering2004-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322004000400002Brazilian Journal of Chemical Engineering v.21 n.4 2004reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322004000400002info:eu-repo/semantics/openAccessFerreira,A. L. O.Giordano,R. L. C.Giordano,R. C.eng2004-10-01T00:00:00Zoai:scielo:S0104-66322004000400002Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2004-10-01T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false
dc.title.none.fl_str_mv Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylase
title Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylase
spellingShingle Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylase
Ferreira,A. L. O.
Ampicillin
immobilized enzyme
beta -lactam antibiotic synthesis
factorial design
title_short Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylase
title_full Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylase
title_fullStr Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylase
title_full_unstemmed Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylase
title_sort Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylase
author Ferreira,A. L. O.
author_facet Ferreira,A. L. O.
Giordano,R. L. C.
Giordano,R. C.
author_role author
author2 Giordano,R. L. C.
Giordano,R. C.
author2_role author
author
dc.contributor.author.fl_str_mv Ferreira,A. L. O.
Giordano,R. L. C.
Giordano,R. C.
dc.subject.por.fl_str_mv Ampicillin
immobilized enzyme
beta -lactam antibiotic synthesis
factorial design
topic Ampicillin
immobilized enzyme
beta -lactam antibiotic synthesis
factorial design
description An experimental design was applied to improve the reaction conditions for enzymatic synthesis of ampicillin from phenylglycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA), catalyzed by penicillin G acylase from E. coli immobilized on an agarose-glyoxyl derivative. The presence and magnitude of interactions between reaction variables were estimated using a 2(5) factorial design. A batch reactor was employed to assess the influence of the following variables: pH, temperature, initial 6-APA concentration, buffer concentration, and the presence of methanol. Response variables were productivity, selectivity, and yield (based on initial 6-APA concentration). The best synthesis yield (56.9%) was at T = 4ºC and pH 6.5. The highest productivity (49.3 ´ 10-3mM of antibiotic/min) was achieved at T = 25ºC and pH 6.5. Our results indicate that it is possible to achieve high productivity for this system while maintaining a high selectivity and yield.
publishDate 2004
dc.date.none.fl_str_mv 2004-12-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322004000400002
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322004000400002
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0104-66322004000400002
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Brazilian Society of Chemical Engineering
publisher.none.fl_str_mv Brazilian Society of Chemical Engineering
dc.source.none.fl_str_mv Brazilian Journal of Chemical Engineering v.21 n.4 2004
reponame:Brazilian Journal of Chemical Engineering
instname:Associação Brasileira de Engenharia Química (ABEQ)
instacron:ABEQ
instname_str Associação Brasileira de Engenharia Química (ABEQ)
instacron_str ABEQ
institution ABEQ
reponame_str Brazilian Journal of Chemical Engineering
collection Brazilian Journal of Chemical Engineering
repository.name.fl_str_mv Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)
repository.mail.fl_str_mv rgiudici@usp.br||rgiudici@usp.br
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