β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: A comparative experimental and modelling study of the galactooligosaccharides production

Detalhes bibliográficos
Autor(a) principal: Neri, D. F. M.
Data de Publicação: 2008
Outros Autores: Balcão, V. M., Costa, Rafael S., Ferreira, Eugénio C., Torres, D., Rodrigues, Lígia M., Carvalho Junior, L. B., Teixeira, J. A.
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://hdl.handle.net/1822/9268
Resumo: β-Galactosidase from Aspergillus oryzae is an enzyme with a wide industrial application, mostly in the hydrolysis of lactose and, more recently, in the synthesis of oligosaccharides. Several advantages are associated with the application of immobilized enzymes on magnetic supports. In this work, β-galactosidase was covalently immobilised onto a Polysiloxane- Polyvinyl Alcohol Magnetic Composite (mPOS-PVA), Magnetic Polysiloxane with Polyaniline (mPOS-PANI), Magnetized Dacron (DACRON) and Magnetite with Polyaniline (MAG-PANI) using glutaraldehyde as activating agent being the synthesis of GOS evaluated and compared at different temperatures (30, 40, 50 and 60 oC) and various initial lactose concentration (50, 100, 200, 300, 400 and 500 g/L). The kinetic parameters obtained by fitting the experimental data were compared in order to determine the effect of the immobilization process with different supports on the synthesis of oligosaccharides. These results clearly demonstrate that all supports may be used for β-galactosidase immobilization as, besides improving the enzyme hydrolytic and GOS synthesis properties, its separation from the obtained reaction products is easy to accomplish.
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spelling β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: A comparative experimental and modelling study of the galactooligosaccharides productionβ-galactosidaseImmobilizationMagnetic supportsGOSMathematical modelingβ-Galactosidase from Aspergillus oryzae is an enzyme with a wide industrial application, mostly in the hydrolysis of lactose and, more recently, in the synthesis of oligosaccharides. Several advantages are associated with the application of immobilized enzymes on magnetic supports. In this work, β-galactosidase was covalently immobilised onto a Polysiloxane- Polyvinyl Alcohol Magnetic Composite (mPOS-PVA), Magnetic Polysiloxane with Polyaniline (mPOS-PANI), Magnetized Dacron (DACRON) and Magnetite with Polyaniline (MAG-PANI) using glutaraldehyde as activating agent being the synthesis of GOS evaluated and compared at different temperatures (30, 40, 50 and 60 oC) and various initial lactose concentration (50, 100, 200, 300, 400 and 500 g/L). The kinetic parameters obtained by fitting the experimental data were compared in order to determine the effect of the immobilization process with different supports on the synthesis of oligosaccharides. These results clearly demonstrate that all supports may be used for β-galactosidase immobilization as, besides improving the enzyme hydrolytic and GOS synthesis properties, its separation from the obtained reaction products is easy to accomplish.Programme Alβan, European Union Programme of High Level Scholarships for Latin AmericaBrazilian National Research Council (CNPq)Universidade do MinhoNeri, D. F. M.Balcão, V. M.Costa, Rafael S.Ferreira, Eugénio C.Torres, D.Rodrigues, Lígia M.Carvalho Junior, L. B.Teixeira, J. A.2008-092008-09-01T00:00:00Zconference paperinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/1822/9268engFERREIRA, E. C. ; MOTA, M., ed. lit. – “Chempor 2008 : proceedings of the International Chemical and Biological Engineering Conference, 10, Braga, 2008”. Braga : Departamento de Engenharia Biológica da Universidade do Minho, 2008. ISBN 97 978-972-97810-3-2. p.1036-1041.978-972-97810-3-2info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-05-11T05:05:34Zoai:repositorium.sdum.uminho.pt:1822/9268Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-11T05:05:34Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: A comparative experimental and modelling study of the galactooligosaccharides production
title β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: A comparative experimental and modelling study of the galactooligosaccharides production
spellingShingle β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: A comparative experimental and modelling study of the galactooligosaccharides production
Neri, D. F. M.
β-galactosidase
Immobilization
Magnetic supports
GOS
Mathematical modeling
title_short β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: A comparative experimental and modelling study of the galactooligosaccharides production
title_full β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: A comparative experimental and modelling study of the galactooligosaccharides production
title_fullStr β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: A comparative experimental and modelling study of the galactooligosaccharides production
title_full_unstemmed β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: A comparative experimental and modelling study of the galactooligosaccharides production
title_sort β-Galactosidase from Aspergillus oryzae immobilized onto different magnetic supports: A comparative experimental and modelling study of the galactooligosaccharides production
author Neri, D. F. M.
author_facet Neri, D. F. M.
Balcão, V. M.
Costa, Rafael S.
Ferreira, Eugénio C.
Torres, D.
Rodrigues, Lígia M.
Carvalho Junior, L. B.
Teixeira, J. A.
author_role author
author2 Balcão, V. M.
Costa, Rafael S.
Ferreira, Eugénio C.
Torres, D.
Rodrigues, Lígia M.
Carvalho Junior, L. B.
Teixeira, J. A.
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Neri, D. F. M.
Balcão, V. M.
Costa, Rafael S.
Ferreira, Eugénio C.
Torres, D.
Rodrigues, Lígia M.
Carvalho Junior, L. B.
Teixeira, J. A.
dc.subject.por.fl_str_mv β-galactosidase
Immobilization
Magnetic supports
GOS
Mathematical modeling
topic β-galactosidase
Immobilization
Magnetic supports
GOS
Mathematical modeling
description β-Galactosidase from Aspergillus oryzae is an enzyme with a wide industrial application, mostly in the hydrolysis of lactose and, more recently, in the synthesis of oligosaccharides. Several advantages are associated with the application of immobilized enzymes on magnetic supports. In this work, β-galactosidase was covalently immobilised onto a Polysiloxane- Polyvinyl Alcohol Magnetic Composite (mPOS-PVA), Magnetic Polysiloxane with Polyaniline (mPOS-PANI), Magnetized Dacron (DACRON) and Magnetite with Polyaniline (MAG-PANI) using glutaraldehyde as activating agent being the synthesis of GOS evaluated and compared at different temperatures (30, 40, 50 and 60 oC) and various initial lactose concentration (50, 100, 200, 300, 400 and 500 g/L). The kinetic parameters obtained by fitting the experimental data were compared in order to determine the effect of the immobilization process with different supports on the synthesis of oligosaccharides. These results clearly demonstrate that all supports may be used for β-galactosidase immobilization as, besides improving the enzyme hydrolytic and GOS synthesis properties, its separation from the obtained reaction products is easy to accomplish.
publishDate 2008
dc.date.none.fl_str_mv 2008-09
2008-09-01T00:00:00Z
dc.type.driver.fl_str_mv conference paper
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://hdl.handle.net/1822/9268
url https://hdl.handle.net/1822/9268
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv FERREIRA, E. C. ; MOTA, M., ed. lit. – “Chempor 2008 : proceedings of the International Chemical and Biological Engineering Conference, 10, Braga, 2008”. Braga : Departamento de Engenharia Biológica da Universidade do Minho, 2008. ISBN 97 978-972-97810-3-2. p.1036-1041.
978-972-97810-3-2
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv mluisa.alvim@gmail.com
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