Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization

Detalhes bibliográficos
Autor(a) principal: Zhan,J. F.
Data de Publicação: 2013
Outros Autores: Jiang,S. T., Pan,L. J.
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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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
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