Improving selectivity and productivity of the enzymatic synthesis of ampicillin with immobilized penicillin G acylase
Autor(a) principal: | |
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Data de Publicação: | 2004 |
Outros Autores: | , |
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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Brazilian Journal of Chemical Engineering |
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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 |
_version_ |
1754213171583778816 |