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|Title:||Immobilization of L-asparaginase towards surface-modified carbon nanotubes|
|Author:||Almeida, Mafalda R.|
Cristóvão, Raquel O.
Barros, Maria A.
Nunes, João C.F.
Boaventura, Rui A. R.
Loureiro, José M.
Faria, Joaquim L.
Santos-Ebinuma, Valéria C.
Tavares, Ana P. M.
Silva, Cláudia G.
|Abstract:||L-asparaginase (ASNase, EC 126.96.36.199) is an enzyme that catalyzes L-asparagine hydrolysis into L-aspartic acid and ammonia and is mainly applied in pharmaceutical and food industries . 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 . Immobilization of ASNase has been proposed as an efficient approach to overcome this limitation . 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.|
|Appears in Collections:||CICECO - Comunicações|
DQ - Comunicações
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