Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate
Autor(a) principal: | |
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Data de Publicação: | 2020 |
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/10773/32941 |
Resumo: | The enzyme L-asparaginase (ASNase) presents effective antineoplastic properties used for acute lymphoblastic leukemia treatment besides their potential use in the food sector to decrease the acrylamide formation. Considering their applications, the improvement of this enzyme's properties by efficient immobilization techniques is in high demand. Carbon nanotubes are promising enzyme immobilization supports, since these materials have increased surface area and effective capacity for enzyme loading. Accordingly, in this study, multi-walled carbon nanotubes (MWCNTs) were explored as novel supports for ASNase immobilization by a simple adsorption method. The effect of pH and contact time of immobilization, as well as the ASNase to nanoparticles mass ratio, were optimized according to the enzyme immobilization yield and relative recovered activity. The enzyme–MWCNTs bioconjugation was confirmed by thermogravimetric analysis (TGA), Fourier transform infrared spectroscopy (FTIR), Raman and transmission electron microscopy (TEM) studies. MWCNTs have a high ASNase loading capacity, with a maximum immobilization yield of 90%. The adsorbed ASNase retains 90% of the initial enzyme activity at the optimized conditions (pH 8.0, 60 min, and 1.5 x 10-3 g mL1 of ASNase). According to these results, ASNase immobilized onto MWCNTs can find improved applications in several areas, namely biosensors, medicine and food industry. |
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Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugateThe enzyme L-asparaginase (ASNase) presents effective antineoplastic properties used for acute lymphoblastic leukemia treatment besides their potential use in the food sector to decrease the acrylamide formation. Considering their applications, the improvement of this enzyme's properties by efficient immobilization techniques is in high demand. Carbon nanotubes are promising enzyme immobilization supports, since these materials have increased surface area and effective capacity for enzyme loading. Accordingly, in this study, multi-walled carbon nanotubes (MWCNTs) were explored as novel supports for ASNase immobilization by a simple adsorption method. The effect of pH and contact time of immobilization, as well as the ASNase to nanoparticles mass ratio, were optimized according to the enzyme immobilization yield and relative recovered activity. The enzyme–MWCNTs bioconjugation was confirmed by thermogravimetric analysis (TGA), Fourier transform infrared spectroscopy (FTIR), Raman and transmission electron microscopy (TEM) studies. MWCNTs have a high ASNase loading capacity, with a maximum immobilization yield of 90%. The adsorbed ASNase retains 90% of the initial enzyme activity at the optimized conditions (pH 8.0, 60 min, and 1.5 x 10-3 g mL1 of ASNase). According to these results, ASNase immobilized onto MWCNTs can find improved applications in several areas, namely biosensors, medicine and food industry.Royal Society of Chemistry2022-01-18T12:20:24Z2020-01-01T00:00:00Z2020info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/32941eng10.1039/D0RA05534DCristóvão, Raquel O.Almeida, Mafalda R.Barros, Maria A.Nunes, João C. F.Boaventura, Rui A. R.Loureiro, José M.Faria, Joaquim L.Neves, Márcia C.Freire, Mara G.Ebinuma-Santos, 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:10773/32941Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:04:21.788302Repositório 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 |
Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate |
title |
Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate |
spellingShingle |
Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate Cristóvão, Raquel O. |
title_short |
Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate |
title_full |
Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate |
title_fullStr |
Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate |
title_full_unstemmed |
Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate |
title_sort |
Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate |
author |
Cristóvão, Raquel O. |
author_facet |
Cristóvão, Raquel O. Almeida, Mafalda R. Barros, Maria A. Nunes, João C. F. Boaventura, Rui A. R. Loureiro, José M. Faria, Joaquim L. Neves, Márcia C. Freire, Mara G. Ebinuma-Santos, Valéria C. Tavares, Ana P. M. Silva, Cláudia G. |
author_role |
author |
author2 |
Almeida, Mafalda R. Barros, Maria A. Nunes, João C. F. Boaventura, Rui A. R. Loureiro, José M. Faria, Joaquim L. Neves, Márcia C. Freire, Mara G. Ebinuma-Santos, 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 |
Cristóvão, Raquel O. Almeida, Mafalda R. Barros, Maria A. Nunes, João C. F. Boaventura, Rui A. R. Loureiro, José M. Faria, Joaquim L. Neves, Márcia C. Freire, Mara G. Ebinuma-Santos, Valéria C. Tavares, Ana P. M. Silva, Cláudia G. |
description |
The enzyme L-asparaginase (ASNase) presents effective antineoplastic properties used for acute lymphoblastic leukemia treatment besides their potential use in the food sector to decrease the acrylamide formation. Considering their applications, the improvement of this enzyme's properties by efficient immobilization techniques is in high demand. Carbon nanotubes are promising enzyme immobilization supports, since these materials have increased surface area and effective capacity for enzyme loading. Accordingly, in this study, multi-walled carbon nanotubes (MWCNTs) were explored as novel supports for ASNase immobilization by a simple adsorption method. The effect of pH and contact time of immobilization, as well as the ASNase to nanoparticles mass ratio, were optimized according to the enzyme immobilization yield and relative recovered activity. The enzyme–MWCNTs bioconjugation was confirmed by thermogravimetric analysis (TGA), Fourier transform infrared spectroscopy (FTIR), Raman and transmission electron microscopy (TEM) studies. MWCNTs have a high ASNase loading capacity, with a maximum immobilization yield of 90%. The adsorbed ASNase retains 90% of the initial enzyme activity at the optimized conditions (pH 8.0, 60 min, and 1.5 x 10-3 g mL1 of ASNase). According to these results, ASNase immobilized onto MWCNTs can find improved applications in several areas, namely biosensors, medicine and food industry. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-01-01T00:00:00Z 2020 2022-01-18T12:20:24Z |
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/10773/32941 |
url |
http://hdl.handle.net/10773/32941 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1039/D0RA05534D |
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 |
Royal Society of Chemistry |
publisher.none.fl_str_mv |
Royal Society of Chemistry |
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 |
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1799137698915549184 |