Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization
Autor(a) principal: | |
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Data de Publicação: | 2013 |
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=S0104-66322013000400004 |
Resumo: | The paper presents the synthesis and performance of an immobilized phospholipase A1 with practical application for oil degumming. The polyvinyl alcohol (PVA) had a number of properties indicating this polymer as a good enzyme carrier. The combination with alginate made a macro-porous structure, evidenced by SEM analyses. When the process time in boric acid solution was 30 minutes, the results revealed that beads prepared with 10% (w/v) PVA and 2% (w/v) sodium alginate in 4% (w/v) boric acid and 2% (w/v) calcium chloride solution exhibited high immobilized enzyme activity, immobilization yield and stability. The pH and temperature optimum for the PVA-alginate immobilized phospholipase A1were 5.6 and 58 °C, respectively. The enzyme immobilized in the beads retained 50.37% of the initial activity in the eighth cycle. The enzyme biocatalyst immobilized in the beads retained 78.58% of the initial activity after storing 6 weeks at 4 °C. |
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oai:scielo:S0104-66322013000400004 |
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Brazilian Journal of Chemical Engineering |
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spelling |
Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilizationPhospholipase A1PVASodium alginateImmobilizationBeads stabilityThe paper presents the synthesis and performance of an immobilized phospholipase A1 with practical application for oil degumming. The polyvinyl alcohol (PVA) had a number of properties indicating this polymer as a good enzyme carrier. The combination with alginate made a macro-porous structure, evidenced by SEM analyses. When the process time in boric acid solution was 30 minutes, the results revealed that beads prepared with 10% (w/v) PVA and 2% (w/v) sodium alginate in 4% (w/v) boric acid and 2% (w/v) calcium chloride solution exhibited high immobilized enzyme activity, immobilization yield and stability. The pH and temperature optimum for the PVA-alginate immobilized phospholipase A1were 5.6 and 58 °C, respectively. The enzyme immobilized in the beads retained 50.37% of the initial activity in the eighth cycle. The enzyme biocatalyst immobilized in the beads retained 78.58% of the initial activity after storing 6 weeks at 4 °C.Brazilian Society of Chemical Engineering2013-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322013000400004Brazilian Journal of Chemical Engineering v.30 n.4 2013reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322013000400004info:eu-repo/semantics/openAccessZhan,J. F.Jiang,S. T.Pan,L. J.eng2014-01-10T00:00:00Zoai:scielo:S0104-66322013000400004Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2014-01-10T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization |
title |
Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization |
spellingShingle |
Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization Zhan,J. F. Phospholipase A1 PVA Sodium alginate Immobilization Beads stability |
title_short |
Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization |
title_full |
Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization |
title_fullStr |
Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization |
title_full_unstemmed |
Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization |
title_sort |
Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization |
author |
Zhan,J. F. |
author_facet |
Zhan,J. F. Jiang,S. T. Pan,L. J. |
author_role |
author |
author2 |
Jiang,S. T. Pan,L. J. |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Zhan,J. F. Jiang,S. T. Pan,L. J. |
dc.subject.por.fl_str_mv |
Phospholipase A1 PVA Sodium alginate Immobilization Beads stability |
topic |
Phospholipase A1 PVA Sodium alginate Immobilization Beads stability |
description |
The paper presents the synthesis and performance of an immobilized phospholipase A1 with practical application for oil degumming. The polyvinyl alcohol (PVA) had a number of properties indicating this polymer as a good enzyme carrier. The combination with alginate made a macro-porous structure, evidenced by SEM analyses. When the process time in boric acid solution was 30 minutes, the results revealed that beads prepared with 10% (w/v) PVA and 2% (w/v) sodium alginate in 4% (w/v) boric acid and 2% (w/v) calcium chloride solution exhibited high immobilized enzyme activity, immobilization yield and stability. The pH and temperature optimum for the PVA-alginate immobilized phospholipase A1were 5.6 and 58 °C, respectively. The enzyme immobilized in the beads retained 50.37% of the initial activity in the eighth cycle. The enzyme biocatalyst immobilized in the beads retained 78.58% of the initial activity after storing 6 weeks at 4 °C. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-12-01 |
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=S0104-66322013000400004 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322013000400004 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-66322013000400004 |
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.30 n.4 2013 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_ |
1754213174213607424 |