Superior operational stability of immobilized l-asparaginase over surface-modified carbon nanotubes

Abstract 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...

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Autores principales:	Mafalda R. Almeida, Raquel O. Cristóvão, Maria A. Barros, João C. F. Nunes, Rui A. R. Boaventura, José M. Loureiro, Joaquim L. Faria, Márcia C. Neves, Mara G. Freire, Valéria C. Santos-Ebinuma, Ana P. M. Tavares, Cláudia G. Silva
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3f5da1c099de4158876e8d4b70b363fa
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spelling	oai:doaj.org-article:3f5da1c099de4158876e8d4b70b363fa2021-11-08T10:51:20ZSuperior operational stability of immobilized l-asparaginase over surface-modified carbon nanotubes10.1038/s41598-021-00841-22045-2322https://doaj.org/article/3f5da1c099de4158876e8d4b70b363fa2021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-00841-2https://doaj.org/toc/2045-2322Abstract 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.Mafalda R. AlmeidaRaquel O. CristóvãoMaria A. BarrosJoão C. F. NunesRui A. R. BoaventuraJosé M. LoureiroJoaquim L. FariaMárcia C. NevesMara G. FreireValéria C. Santos-EbinumaAna P. M. TavaresCláudia G. SilvaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mafalda R. Almeida Raquel O. Cristóvão Maria A. Barros João C. F. Nunes Rui A. R. Boaventura José M. Loureiro Joaquim L. Faria Márcia C. Neves Mara G. Freire Valéria C. Santos-Ebinuma Ana P. M. Tavares Cláudia G. Silva Superior operational stability of immobilized l-asparaginase over surface-modified carbon nanotubes
description	Abstract 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.
format	article
author	Mafalda R. Almeida Raquel O. Cristóvão Maria A. Barros João C. F. Nunes Rui A. R. Boaventura José M. Loureiro Joaquim L. Faria Márcia C. Neves Mara G. Freire Valéria C. Santos-Ebinuma Ana P. M. Tavares Cláudia G. Silva
author_facet	Mafalda R. Almeida Raquel O. Cristóvão Maria A. Barros João C. F. Nunes Rui A. R. Boaventura José M. Loureiro Joaquim L. Faria Márcia C. Neves Mara G. Freire Valéria C. Santos-Ebinuma Ana P. M. Tavares Cláudia G. Silva
author_sort	Mafalda R. Almeida
title	Superior operational stability of immobilized l-asparaginase over surface-modified carbon nanotubes
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
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/3f5da1c099de4158876e8d4b70b363fa
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Superior operational stability of immobilized l-asparaginase over surface-modified carbon nanotubes

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