MULTI-POINT IMMOBILIZATION OF PENICILLIN G ACYLASE ON SILICA-GLYOXYL: INFLUENCE OF THE DEGREE OF ACTIVATION
Autor(a) principal: | |
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Data de Publicação: | 1997 |
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=S0104-66321997000400005 |
Resumo: | Multi-point immobilization, by an intense enzyme-support attachment, may increase the operational stability of a biocatalyst. Penicillin G acylase has many applications, from the hydrolysis of penicillin G (production of 6-aminopenicillanic acid) to the synthesis of semi-synthetic antibiotics. The application of this technique in macroporous silica involves support activation with 3-glycidyloxypropyltrimetoxysilane, followed by acidic hydrolysis and oxidation with sodium periodate. The aldehyde-glyoxyl groups so formed react subsequently with the enzyme. The degree of activation affects the yield and stability of the enzyme immobilization. For 20 UI of enzyme, the results show an immobilization yield equal to 100%, whenever there are more than 140 <FONT FACE="Symbol">m</FONT> Eq of aldehyde groups/g of dry silica. The immobilized enzyme half-life is 23 minutes at 60ºC; under the same conditions, the soluble enzyme has no residual activity after a few minutes. The increase in the degree of activation does not lead to higher stability, which indicates the negative influence of sub-products, formed during the activation of the support |
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Brazilian Journal of Chemical Engineering |
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MULTI-POINT IMMOBILIZATION OF PENICILLIN G ACYLASE ON SILICA-GLYOXYL: INFLUENCE OF THE DEGREE OF ACTIVATIONMulti-point immobilizationbiocatalystsilicaMulti-point immobilization, by an intense enzyme-support attachment, may increase the operational stability of a biocatalyst. Penicillin G acylase has many applications, from the hydrolysis of penicillin G (production of 6-aminopenicillanic acid) to the synthesis of semi-synthetic antibiotics. The application of this technique in macroporous silica involves support activation with 3-glycidyloxypropyltrimetoxysilane, followed by acidic hydrolysis and oxidation with sodium periodate. The aldehyde-glyoxyl groups so formed react subsequently with the enzyme. The degree of activation affects the yield and stability of the enzyme immobilization. For 20 UI of enzyme, the results show an immobilization yield equal to 100%, whenever there are more than 140 <FONT FACE="Symbol">m</FONT> Eq of aldehyde groups/g of dry silica. The immobilized enzyme half-life is 23 minutes at 60ºC; under the same conditions, the soluble enzyme has no residual activity after a few minutes. The increase in the degree of activation does not lead to higher stability, which indicates the negative influence of sub-products, formed during the activation of the supportBrazilian Society of Chemical Engineering1997-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66321997000400005Brazilian Journal of Chemical Engineering v.14 n.4 1997reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66321997000400005info:eu-repo/semantics/openAccessPEREIRA,G.H.A.GUISÁN,J.M.GIORDANO,R.L.C.eng1998-10-06T00:00:00Zoai:scielo:S0104-66321997000400005Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:1998-10-06T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
MULTI-POINT IMMOBILIZATION OF PENICILLIN G ACYLASE ON SILICA-GLYOXYL: INFLUENCE OF THE DEGREE OF ACTIVATION |
title |
MULTI-POINT IMMOBILIZATION OF PENICILLIN G ACYLASE ON SILICA-GLYOXYL: INFLUENCE OF THE DEGREE OF ACTIVATION |
spellingShingle |
MULTI-POINT IMMOBILIZATION OF PENICILLIN G ACYLASE ON SILICA-GLYOXYL: INFLUENCE OF THE DEGREE OF ACTIVATION PEREIRA,G.H.A. Multi-point immobilization biocatalyst silica |
title_short |
MULTI-POINT IMMOBILIZATION OF PENICILLIN G ACYLASE ON SILICA-GLYOXYL: INFLUENCE OF THE DEGREE OF ACTIVATION |
title_full |
MULTI-POINT IMMOBILIZATION OF PENICILLIN G ACYLASE ON SILICA-GLYOXYL: INFLUENCE OF THE DEGREE OF ACTIVATION |
title_fullStr |
MULTI-POINT IMMOBILIZATION OF PENICILLIN G ACYLASE ON SILICA-GLYOXYL: INFLUENCE OF THE DEGREE OF ACTIVATION |
title_full_unstemmed |
MULTI-POINT IMMOBILIZATION OF PENICILLIN G ACYLASE ON SILICA-GLYOXYL: INFLUENCE OF THE DEGREE OF ACTIVATION |
title_sort |
MULTI-POINT IMMOBILIZATION OF PENICILLIN G ACYLASE ON SILICA-GLYOXYL: INFLUENCE OF THE DEGREE OF ACTIVATION |
author |
PEREIRA,G.H.A. |
author_facet |
PEREIRA,G.H.A. GUISÁN,J.M. GIORDANO,R.L.C. |
author_role |
author |
author2 |
GUISÁN,J.M. GIORDANO,R.L.C. |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
PEREIRA,G.H.A. GUISÁN,J.M. GIORDANO,R.L.C. |
dc.subject.por.fl_str_mv |
Multi-point immobilization biocatalyst silica |
topic |
Multi-point immobilization biocatalyst silica |
description |
Multi-point immobilization, by an intense enzyme-support attachment, may increase the operational stability of a biocatalyst. Penicillin G acylase has many applications, from the hydrolysis of penicillin G (production of 6-aminopenicillanic acid) to the synthesis of semi-synthetic antibiotics. The application of this technique in macroporous silica involves support activation with 3-glycidyloxypropyltrimetoxysilane, followed by acidic hydrolysis and oxidation with sodium periodate. The aldehyde-glyoxyl groups so formed react subsequently with the enzyme. The degree of activation affects the yield and stability of the enzyme immobilization. For 20 UI of enzyme, the results show an immobilization yield equal to 100%, whenever there are more than 140 <FONT FACE="Symbol">m</FONT> Eq of aldehyde groups/g of dry silica. The immobilized enzyme half-life is 23 minutes at 60ºC; under the same conditions, the soluble enzyme has no residual activity after a few minutes. The increase in the degree of activation does not lead to higher stability, which indicates the negative influence of sub-products, formed during the activation of the support |
publishDate |
1997 |
dc.date.none.fl_str_mv |
1997-12-01 |
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=S0104-66321997000400005 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66321997000400005 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-66321997000400005 |
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.14 n.4 1997 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_ |
1754213170306613248 |