Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports
Autor(a) principal: | |
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Data de Publicação: | 2001 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.14/6833 |
Resumo: | In the present research work, production of coimmobilized derivatives of L-asparaginase and glutamate dehydrogenase was attempted. Comparison of immobilization of each enzyme independently with coimmobilization of the two enzymes unfolded important advantages of the latter, namely a decrease in the induction period (time before the maximum reaction rate is virtually achieved) and an increase in the maximum reaction rate. The effectiveness of the independent enzyme derivatives was low; however, it was enhanced by three-fold when the enzymes were coimmobilized onto the same agarose-glutaraldehyde support. Each supporting agarose bead may in fact be viewed as a nano-reactor with in situ reaction and separation (i.e. elimination of the ammonia formed), with the nanoenvironment surrounding each enzyme molecule being essentially devoid of steric hindrance. |
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Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supportsEnzymeAgaroseStructural stabilizationImmobilizationBiochemical engineeringBiomedical engineeringIn the present research work, production of coimmobilized derivatives of L-asparaginase and glutamate dehydrogenase was attempted. Comparison of immobilization of each enzyme independently with coimmobilization of the two enzymes unfolded important advantages of the latter, namely a decrease in the induction period (time before the maximum reaction rate is virtually achieved) and an increase in the maximum reaction rate. The effectiveness of the independent enzyme derivatives was low; however, it was enhanced by three-fold when the enzymes were coimmobilized onto the same agarose-glutaraldehyde support. Each supporting agarose bead may in fact be viewed as a nano-reactor with in situ reaction and separation (i.e. elimination of the ammonia formed), with the nanoenvironment surrounding each enzyme molecule being essentially devoid of steric hindrance.Veritati - Repositório Institucional da Universidade Católica PortuguesaBalcão, Victor M.Mateo, CesarFernández-Lafuente, R.Malcata, F. XavierGuisán, José M.2011-10-22T16:02:22Z20012001-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/6833engBALCÃO, Vitor M... [et al.] - Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports. Enzyme and Microbial Technology. ISSN 0141-0229. Vol. 28, n.º 7-8 (2001), p. 696–70410.1016/S0141-0229(01)00307-6info: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:RCAAP2023-07-12T17:10:35Zoai:repositorio.ucp.pt:10400.14/6833Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:05:50.214257Repositório 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 |
Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports |
title |
Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports |
spellingShingle |
Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports Balcão, Victor M. Enzyme Agarose Structural stabilization Immobilization Biochemical engineering Biomedical engineering |
title_short |
Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports |
title_full |
Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports |
title_fullStr |
Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports |
title_full_unstemmed |
Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports |
title_sort |
Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports |
author |
Balcão, Victor M. |
author_facet |
Balcão, Victor M. Mateo, Cesar Fernández-Lafuente, R. Malcata, F. Xavier Guisán, José M. |
author_role |
author |
author2 |
Mateo, Cesar Fernández-Lafuente, R. Malcata, F. Xavier Guisán, José M. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Veritati - Repositório Institucional da Universidade Católica Portuguesa |
dc.contributor.author.fl_str_mv |
Balcão, Victor M. Mateo, Cesar Fernández-Lafuente, R. Malcata, F. Xavier Guisán, José M. |
dc.subject.por.fl_str_mv |
Enzyme Agarose Structural stabilization Immobilization Biochemical engineering Biomedical engineering |
topic |
Enzyme Agarose Structural stabilization Immobilization Biochemical engineering Biomedical engineering |
description |
In the present research work, production of coimmobilized derivatives of L-asparaginase and glutamate dehydrogenase was attempted. Comparison of immobilization of each enzyme independently with coimmobilization of the two enzymes unfolded important advantages of the latter, namely a decrease in the induction period (time before the maximum reaction rate is virtually achieved) and an increase in the maximum reaction rate. The effectiveness of the independent enzyme derivatives was low; however, it was enhanced by three-fold when the enzymes were coimmobilized onto the same agarose-glutaraldehyde support. Each supporting agarose bead may in fact be viewed as a nano-reactor with in situ reaction and separation (i.e. elimination of the ammonia formed), with the nanoenvironment surrounding each enzyme molecule being essentially devoid of steric hindrance. |
publishDate |
2001 |
dc.date.none.fl_str_mv |
2001 2001-01-01T00:00:00Z 2011-10-22T16:02:22Z |
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 |
http://hdl.handle.net/10400.14/6833 |
url |
http://hdl.handle.net/10400.14/6833 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
BALCÃO, Vitor M... [et al.] - Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports. Enzyme and Microbial Technology. ISSN 0141-0229. Vol. 28, n.º 7-8 (2001), p. 696–704 10.1016/S0141-0229(01)00307-6 |
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 |
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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 |
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