Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes
Autor(a) principal: | |
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Data de Publicação: | 2021 |
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/10773/32920 |
Resumo: | L-asparaginase (ASNase, EC 3.5.1.1) is an enzyme that catalyzes the L-asparagine hydrolysis into L-aspartic acid and ammonia, being mainly applied in pharmaceutical and food industries. However, some disadvantages are associated with its free form, such as the ASNase short half-life, which may be overcome by enzyme immobilization. In this work, the immobilization of ASNase by adsorption over pristine and modified multi-walled carbon nanotubes (MWCNTs) was investigated, the latter corresponding to functionalized MWCNTs through a hydrothermal oxidation treatment. Different operating conditions, including pH, contact time and ASNase/MWCNT mass ratio, as well as the operational stability of the immobilized ASNase, were evaluated. For comparison purposes, data regarding the ASNase immobilization with pristine MWCNT was detailed. The characterization of the ASNase-MWCNT bioconjugate was addressed using different techniques, namely Transmission Electron Microscopy (TEM), Thermogravimetric Analysis (TGA) and Raman spectroscopy. Functionalized MWCNTs showed promising results, with an immobilization yield and a relative recovered activity of commercial ASNase above 95% under the optimized adsorption conditions (pH 8, 60 min of contact and 1.5 × 10-3 g mL-1 of ASNase). The ASNase-MWCNT bioconjugate also showed improved enzyme operational stability (6 consecutive reaction cycles without activity loss), paving the way for its use in industrial processes. |
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Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubesL-asparaginase (ASNase, EC 3.5.1.1) is an enzyme that catalyzes the L-asparagine hydrolysis into L-aspartic acid and ammonia, being mainly applied in pharmaceutical and food industries. However, some disadvantages are associated with its free form, such as the ASNase short half-life, which may be overcome by enzyme immobilization. In this work, the immobilization of ASNase by adsorption over pristine and modified multi-walled carbon nanotubes (MWCNTs) was investigated, the latter corresponding to functionalized MWCNTs through a hydrothermal oxidation treatment. Different operating conditions, including pH, contact time and ASNase/MWCNT mass ratio, as well as the operational stability of the immobilized ASNase, were evaluated. For comparison purposes, data regarding the ASNase immobilization with pristine MWCNT was detailed. The characterization of the ASNase-MWCNT bioconjugate was addressed using different techniques, namely Transmission Electron Microscopy (TEM), Thermogravimetric Analysis (TGA) and Raman spectroscopy. Functionalized MWCNTs showed promising results, with an immobilization yield and a relative recovered activity of commercial ASNase above 95% under the optimized adsorption conditions (pH 8, 60 min of contact and 1.5 × 10-3 g mL-1 of ASNase). The ASNase-MWCNT bioconjugate also showed improved enzyme operational stability (6 consecutive reaction cycles without activity loss), paving the way for its use in industrial processes.Nature Research2022-01-13T16:43:19Z2021-12-01T00:00:00Z2021-12info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/32920eng10.1038/s41598-021-00841-2Almeida, Mafalda R.Cristóvão, Raquel O.Barros, Maria A.Nunes, João C. F.Boaventura, Rui A. R.Loureiro, José M.Faria, Joaquim L.Neves, Márcia C.Freire, Mara G.Santos-Ebinuma, Valéria C.Tavares, Ana P. M.Silva, Cláudia G.info: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:RCAAP2024-02-22T12:03:09Zoai:ria.ua.pt:10773/32920Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:04:21.580326Repositório 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 |
Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes |
title |
Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes |
spellingShingle |
Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes Almeida, Mafalda R. |
title_short |
Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes |
title_full |
Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes |
title_fullStr |
Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes |
title_full_unstemmed |
Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes |
title_sort |
Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes |
author |
Almeida, Mafalda R. |
author_facet |
Almeida, Mafalda R. Cristóvão, Raquel O. Barros, Maria A. Nunes, João C. F. Boaventura, Rui A. R. Loureiro, José M. Faria, Joaquim L. Neves, Márcia C. Freire, Mara G. Santos-Ebinuma, Valéria C. Tavares, Ana P. M. Silva, Cláudia G. |
author_role |
author |
author2 |
Cristóvão, Raquel O. Barros, Maria A. Nunes, João C. F. Boaventura, Rui A. R. Loureiro, José M. Faria, Joaquim L. Neves, Márcia C. Freire, Mara G. Santos-Ebinuma, Valéria C. Tavares, Ana P. M. Silva, Cláudia G. |
author2_role |
author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Almeida, Mafalda R. Cristóvão, Raquel O. Barros, Maria A. Nunes, João C. F. Boaventura, Rui A. R. Loureiro, José M. Faria, Joaquim L. Neves, Márcia C. Freire, Mara G. Santos-Ebinuma, Valéria C. Tavares, Ana P. M. Silva, Cláudia G. |
description |
L-asparaginase (ASNase, EC 3.5.1.1) is an enzyme that catalyzes the L-asparagine hydrolysis into L-aspartic acid and ammonia, being mainly applied in pharmaceutical and food industries. However, some disadvantages are associated with its free form, such as the ASNase short half-life, which may be overcome by enzyme immobilization. In this work, the immobilization of ASNase by adsorption over pristine and modified multi-walled carbon nanotubes (MWCNTs) was investigated, the latter corresponding to functionalized MWCNTs through a hydrothermal oxidation treatment. Different operating conditions, including pH, contact time and ASNase/MWCNT mass ratio, as well as the operational stability of the immobilized ASNase, were evaluated. For comparison purposes, data regarding the ASNase immobilization with pristine MWCNT was detailed. The characterization of the ASNase-MWCNT bioconjugate was addressed using different techniques, namely Transmission Electron Microscopy (TEM), Thermogravimetric Analysis (TGA) and Raman spectroscopy. Functionalized MWCNTs showed promising results, with an immobilization yield and a relative recovered activity of commercial ASNase above 95% under the optimized adsorption conditions (pH 8, 60 min of contact and 1.5 × 10-3 g mL-1 of ASNase). The ASNase-MWCNT bioconjugate also showed improved enzyme operational stability (6 consecutive reaction cycles without activity loss), paving the way for its use in industrial processes. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-12-01T00:00:00Z 2021-12 2022-01-13T16:43:19Z |
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/10773/32920 |
url |
http://hdl.handle.net/10773/32920 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1038/s41598-021-00841-2 |
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.publisher.none.fl_str_mv |
Nature Research |
publisher.none.fl_str_mv |
Nature Research |
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 |
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1799137698909257728 |