Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis

Detalhes bibliográficos
Autor(a) principal: Neri, D. F. M.
Data de Publicação: 2008
Outros Autores: Balcão, V. M., Carneiro-da-Cunha, Maria G., Carvalho Junior, L. B., Teixeira, J. A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://hdl.handle.net/1822/8158
Resumo: β-Galactosidase from Kluyveromyces lactis was covalently immobilized onto a mPOS–PVA, using glutaraldehyde as activating agent and its properties were evaluated. The enzymatic water insoluble derivative displayed the same optimum pH (6.5) and optimum temperature (50 °C) of the soluble enzyme. The apparent Km app and activation energy for both soluble and immobilized enzyme derivative were found to be not significantly different. The mPOS–PVA β-galactosidase preparation presented a higher operational and thermal stability than the soluble enzyme. This immobilized β-galactosidase also was effective in hydrolyzing lactose from milk. Hence, one can conclude that mPOS–PVA is an attractive and efficient support for β-galactosidase immobilization.
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spelling Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysisb-GalactosidaseKluyveromyces lactisCovalent immobilizationPolysiloxanePolyvinyl alcoholMagnetic supportβ-GalactosidaseScience & Technologyβ-Galactosidase from Kluyveromyces lactis was covalently immobilized onto a mPOS–PVA, using glutaraldehyde as activating agent and its properties were evaluated. The enzymatic water insoluble derivative displayed the same optimum pH (6.5) and optimum temperature (50 °C) of the soluble enzyme. The apparent Km app and activation energy for both soluble and immobilized enzyme derivative were found to be not significantly different. The mPOS–PVA β-galactosidase preparation presented a higher operational and thermal stability than the soluble enzyme. This immobilized β-galactosidase also was effective in hydrolyzing lactose from milk. Hence, one can conclude that mPOS–PVA is an attractive and efficient support for β-galactosidase immobilization.Alban, the European Union Programme of High Level Scholarships for Latin America; Brazilian National Research Council (CNPq).Elsevier B.V.Universidade do MinhoNeri, D. F. M.Balcão, V. M.Carneiro-da-Cunha, Maria G.Carvalho Junior, L. B.Teixeira, J. A.2008-082008-08-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/1822/8158eng"Catalysis Communications". ISSN 1566-7367. 9:14 (Aug. 2008) 2334-2339.1566-736710.1016/j.catcom.2008.05.022info: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:RCAAP2023-07-21T12:09:07ZPortal AgregadorONG
dc.title.none.fl_str_mv Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis
title Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis
spellingShingle Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis
Neri, D. F. M.
b-Galactosidase
Kluyveromyces lactis
Covalent immobilization
Polysiloxane
Polyvinyl alcohol
Magnetic support
β-Galactosidase
Science & Technology
title_short Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis
title_full Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis
title_fullStr Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis
title_full_unstemmed Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis
title_sort Immobilization of b-galactosidase from kluyveromyces lactis onto a polysiloxane–polyvinyl alcohol magnetic (mPOS–PVA) composite for lactose hydrolysis
author Neri, D. F. M.
author_facet Neri, D. F. M.
Balcão, V. M.
Carneiro-da-Cunha, Maria G.
Carvalho Junior, L. B.
Teixeira, J. A.
author_role author
author2 Balcão, V. M.
Carneiro-da-Cunha, Maria G.
Carvalho Junior, L. B.
Teixeira, J. A.
author2_role 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.
Carneiro-da-Cunha, Maria G.
Carvalho Junior, L. B.
Teixeira, J. A.
dc.subject.por.fl_str_mv b-Galactosidase
Kluyveromyces lactis
Covalent immobilization
Polysiloxane
Polyvinyl alcohol
Magnetic support
β-Galactosidase
Science & Technology
topic b-Galactosidase
Kluyveromyces lactis
Covalent immobilization
Polysiloxane
Polyvinyl alcohol
Magnetic support
β-Galactosidase
Science & Technology
description β-Galactosidase from Kluyveromyces lactis was covalently immobilized onto a mPOS–PVA, using glutaraldehyde as activating agent and its properties were evaluated. The enzymatic water insoluble derivative displayed the same optimum pH (6.5) and optimum temperature (50 °C) of the soluble enzyme. The apparent Km app and activation energy for both soluble and immobilized enzyme derivative were found to be not significantly different. The mPOS–PVA β-galactosidase preparation presented a higher operational and thermal stability than the soluble enzyme. This immobilized β-galactosidase also was effective in hydrolyzing lactose from milk. Hence, one can conclude that mPOS–PVA is an attractive and efficient support for β-galactosidase immobilization.
publishDate 2008
dc.date.none.fl_str_mv 2008-08
2008-08-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://hdl.handle.net/1822/8158
url https://hdl.handle.net/1822/8158
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv "Catalysis Communications". ISSN 1566-7367. 9:14 (Aug. 2008) 2334-2339.
1566-7367
10.1016/j.catcom.2008.05.022
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.publisher.none.fl_str_mv Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
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)
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