Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis
Autor(a) principal: | |
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Data de Publicação: | 2012 |
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=S0104-66322012000100002 |
Resumo: | The immobilization of Aspergillus oryzae β-galactosidase was achieved by entrapment in sodium alginate and gelatin and cross-linking with glutaraldehyde. The optimal concentrations of the aforementioned variables in the immobilization process were determined using an orthogonal central composite design with an orthogonal axial value of 1.35313. The concentrations of alginate, gelatin and glutaraldehyde that provided the greatest enzymatic activity were 6.60%, 4.05% and 3.64% (w/v), respectively. The stability of the immobilized enzyme under the optimal conditions was evaluated through daily activity assays. After 25 uses, a 20% decrease in the enzymatic activity was observed, indicating that the immobilization process could be used to produce a stable biocatalyst. This study investigates the influence of lactose and product concentrations on kinetic reaction hydrolysis. The concentration ranges for the studied variables were 10 to 56 g/L for lactose and 0 to 11.5 g/L for glucose and galactose. Only galactose presented a competitive inhibitory effect. |
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Brazilian Journal of Chemical Engineering |
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Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysisAlginateAspergillus oryzaeβ-galactosidase enzymeEntrapmentOptimization, GelatinThe immobilization of Aspergillus oryzae β-galactosidase was achieved by entrapment in sodium alginate and gelatin and cross-linking with glutaraldehyde. The optimal concentrations of the aforementioned variables in the immobilization process were determined using an orthogonal central composite design with an orthogonal axial value of 1.35313. The concentrations of alginate, gelatin and glutaraldehyde that provided the greatest enzymatic activity were 6.60%, 4.05% and 3.64% (w/v), respectively. The stability of the immobilized enzyme under the optimal conditions was evaluated through daily activity assays. After 25 uses, a 20% decrease in the enzymatic activity was observed, indicating that the immobilization process could be used to produce a stable biocatalyst. This study investigates the influence of lactose and product concentrations on kinetic reaction hydrolysis. The concentration ranges for the studied variables were 10 to 56 g/L for lactose and 0 to 11.5 g/L for glucose and galactose. Only galactose presented a competitive inhibitory effect.Brazilian Society of Chemical Engineering2012-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322012000100002Brazilian Journal of Chemical Engineering v.29 n.1 2012reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322012000100002info:eu-repo/semantics/openAccessFreitas,F. F.Marquez,L. D. S.Ribeiro,G. P.Brandão,G. C.Cardoso,V. L.Ribeiro,E. J.eng2012-03-08T00:00:00Zoai:scielo:S0104-66322012000100002Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2012-03-08T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis |
title |
Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis |
spellingShingle |
Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis Freitas,F. F. Alginate Aspergillus oryzae β-galactosidase enzyme Entrapment Optimization, Gelatin |
title_short |
Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis |
title_full |
Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis |
title_fullStr |
Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis |
title_full_unstemmed |
Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis |
title_sort |
Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis |
author |
Freitas,F. F. |
author_facet |
Freitas,F. F. Marquez,L. D. S. Ribeiro,G. P. Brandão,G. C. Cardoso,V. L. Ribeiro,E. J. |
author_role |
author |
author2 |
Marquez,L. D. S. Ribeiro,G. P. Brandão,G. C. Cardoso,V. L. Ribeiro,E. J. |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Freitas,F. F. Marquez,L. D. S. Ribeiro,G. P. Brandão,G. C. Cardoso,V. L. Ribeiro,E. J. |
dc.subject.por.fl_str_mv |
Alginate Aspergillus oryzae β-galactosidase enzyme Entrapment Optimization, Gelatin |
topic |
Alginate Aspergillus oryzae β-galactosidase enzyme Entrapment Optimization, Gelatin |
description |
The immobilization of Aspergillus oryzae β-galactosidase was achieved by entrapment in sodium alginate and gelatin and cross-linking with glutaraldehyde. The optimal concentrations of the aforementioned variables in the immobilization process were determined using an orthogonal central composite design with an orthogonal axial value of 1.35313. The concentrations of alginate, gelatin and glutaraldehyde that provided the greatest enzymatic activity were 6.60%, 4.05% and 3.64% (w/v), respectively. The stability of the immobilized enzyme under the optimal conditions was evaluated through daily activity assays. After 25 uses, a 20% decrease in the enzymatic activity was observed, indicating that the immobilization process could be used to produce a stable biocatalyst. This study investigates the influence of lactose and product concentrations on kinetic reaction hydrolysis. The concentration ranges for the studied variables were 10 to 56 g/L for lactose and 0 to 11.5 g/L for glucose and galactose. Only galactose presented a competitive inhibitory effect. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-03-01 |
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=S0104-66322012000100002 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322012000100002 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-66322012000100002 |
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.29 n.1 2012 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_ |
1754213173516304384 |