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DC Field | Value | Language |
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dc.contributor.author | Almeida, Mafalda R. | pt_PT |
dc.contributor.author | Cristóvão, Raquel O. | pt_PT |
dc.contributor.author | Barros, Maria A. | pt_PT |
dc.contributor.author | Nunes, João C.F. | pt_PT |
dc.contributor.author | Boaventura, Rui A. R. | pt_PT |
dc.contributor.author | Loureiro, José M. | pt_PT |
dc.contributor.author | Faria, Joaquim L. | pt_PT |
dc.contributor.author | Neves, Márcia | pt_PT |
dc.contributor.author | Santos-Ebinuma, Valéria C. | pt_PT |
dc.contributor.author | Tavares, Ana P. M. | pt_PT |
dc.contributor.author | Silva, Cláudia G. | pt_PT |
dc.date.accessioned | 2022-01-19T14:21:19Z | - |
dc.date.available | 2022-01-19T14:21:19Z | - |
dc.date.issued | 2021 | - |
dc.identifier.uri | http://hdl.handle.net/10773/32964 | - |
dc.description.abstract | L-asparaginase (ASNase, EC 3.5.1.1) is an enzyme that catalyzes L-asparagine hydrolysis into L-aspartic acid and ammonia and is mainly applied in pharmaceutical and food industries [1]. The ASNase currently commercialized for pharmaceutical purposes is produced from two main bacterial sources: recombinant Escherichia coli and Erwinia chrysanthemi. However, some disadvantages are associated with its free form, such as the shorter half-life [2]. Immobilization of ASNase has been proposed as an efficient approach to overcome this limitation [3]. In this work, a straightforward method, including the functionalization of multi-walled carbon nanotubes (MWCNTs) through a hydrothermal oxidation treatment with nitric acid, and the immobilization of ASNase by adsorption over pristine and modified MWCNTs was investigated. Different operation conditions, including pH, contact time, ASNase/MWCNT mass ratio, and the operational stability of the immobilized ASNase were evaluated. 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-1of ASNase). The ASNase-MWCNT bioconjugate also showed improved enzyme operational stability (6 consecutive reaction cycles without activity loss), proving its suitability for application in industrial processes. | pt_PT |
dc.language.iso | eng | pt_PT |
dc.relation | POCI-01-0145-FEDER-031268 | pt_PT |
dc.relation | UIDB/50011/2020 | pt_PT |
dc.relation | UIDP/50011/2020 | pt_PT |
dc.relation | UIDB/EQU/50020/2020 | pt_PT |
dc.relation | CEECIND/00383/2017 | pt_PT |
dc.relation | 2018/06908-8 | pt_PT |
dc.relation | IF/01634/2015 | pt_PT |
dc.relation | DL57/2016 | pt_PT |
dc.rights | openAccess | pt_PT |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | pt_PT |
dc.title | Immobilization of L-asparaginase towards surface-modified carbon nanotubes | pt_PT |
dc.type | conferenceObject | pt_PT |
dc.description.version | published | pt_PT |
dc.peerreviewed | no | pt_PT |
ua.event.date | 22-24 junho, 2021 | pt_PT |
degois.publication.title | Affinity 2021: The 24th meeting of the International Society for Molecular Recognition | pt_PT |
Appears in Collections: | CICECO - Comunicações DQ - Comunicações |
Files in This Item:
File | Description | Size | Format | |
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Abstract_Mafalda.pdf | 46.1 kB | Adobe PDF | View/Open |
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