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 Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1039/d0ra05534d http://hdl.handle.net/11449/199400 |
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 × 10-3 g mL-1 of ASNase). According to these results, ASNase immobilized onto MWCNTs can find improved applications in several areas, namely biosensors, medicine and food industry. This journal is |
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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 × 10-3 g mL-1 of ASNase). According to these results, ASNase immobilized onto MWCNTs can find improved applications in several areas, namely biosensors, medicine and food industry. This journal isLaboratory of Separation and Reaction Engineering-Laboratory of Catalysis and Materials (LSRE-LCM) Department of Chemical Engineering Faculty of Engineering University of Porto, Rua Dr Roberto FriasDepartment of Chemistry CICECO-Aveiro Institute of Materials University of AveiroDepartment of Engineering Bioprocess and Biotechnology School of Pharmaceutical Sciences UNESP-University Estadual PaulistaDepartment of Engineering Bioprocess and Biotechnology School of Pharmaceutical Sciences UNESP-University Estadual PaulistaUniversity of PortoUniversity of AveiroUniversidade Estadual Paulista (Unesp)Cristovao, Raquel O.Almeida, Mafalda R.Barros, Maria A.Nunes, Joao C. F.Boaventura, Rui A. R.Loureiro, Jose M.Faria, Joaquim L.Neves, Marcia C.Freire, Mara G.Ebinuma-Santos, Valeria C. [UNESP]Tavares, Ana P. M.Silva, Claudia G.2020-12-12T01:38:47Z2020-12-12T01:38:47Z2020-08-24info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article31205-31213http://dx.doi.org/10.1039/d0ra05534dRSC Advances, v. 10, n. 52, p. 31205-31213, 2020.2046-2069http://hdl.handle.net/11449/19940010.1039/d0ra05534d2-s2.0-85091009232Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengRSC Advancesinfo:eu-repo/semantics/openAccess2021-10-22T20:42:35Zoai:repositorio.unesp.br:11449/199400Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-22T20:42:35Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
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 Cristovao, 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 |
Cristovao, Raquel O. |
author_facet |
Cristovao, Raquel O. Almeida, Mafalda R. Barros, Maria A. Nunes, Joao C. F. Boaventura, Rui A. R. Loureiro, Jose M. Faria, Joaquim L. Neves, Marcia C. Freire, Mara G. Ebinuma-Santos, Valeria C. [UNESP] Tavares, Ana P. M. Silva, Claudia G. |
author_role |
author |
author2 |
Almeida, Mafalda R. Barros, Maria A. Nunes, Joao C. F. Boaventura, Rui A. R. Loureiro, Jose M. Faria, Joaquim L. Neves, Marcia C. Freire, Mara G. Ebinuma-Santos, Valeria C. [UNESP] Tavares, Ana P. M. Silva, Claudia G. |
author2_role |
author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
University of Porto University of Aveiro Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Cristovao, Raquel O. Almeida, Mafalda R. Barros, Maria A. Nunes, Joao C. F. Boaventura, Rui A. R. Loureiro, Jose M. Faria, Joaquim L. Neves, Marcia C. Freire, Mara G. Ebinuma-Santos, Valeria C. [UNESP] Tavares, Ana P. M. Silva, Claudia 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 × 10-3 g mL-1 of ASNase). According to these results, ASNase immobilized onto MWCNTs can find improved applications in several areas, namely biosensors, medicine and food industry. This journal is |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-12-12T01:38:47Z 2020-12-12T01:38:47Z 2020-08-24 |
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://dx.doi.org/10.1039/d0ra05534d RSC Advances, v. 10, n. 52, p. 31205-31213, 2020. 2046-2069 http://hdl.handle.net/11449/199400 10.1039/d0ra05534d 2-s2.0-85091009232 |
url |
http://dx.doi.org/10.1039/d0ra05534d http://hdl.handle.net/11449/199400 |
identifier_str_mv |
RSC Advances, v. 10, n. 52, p. 31205-31213, 2020. 2046-2069 10.1039/d0ra05534d 2-s2.0-85091009232 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
RSC Advances |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
31205-31213 |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
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1799965741515014144 |