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

Autor(es):Mostrar menos -

Almeida, Mafalda R. ^[1] ; Cristovao, Raquel O. ^[2] ; Barros, Maria A. ^[2] ; Nunes, Joao C. F. ^[1] ; Boaventura, Rui A. R. ^[2] ; Loureiro, Jose M. ^[2] ; Faria, Joaquim L. ^[2] ; Neves, Marcia C. ^[1] ; Freire, Mara G. ^[1] ; Santos-Ebinuma, Valeria C. ^[3] ; Tavares, Ana P. M. ^[1] ; Silva, Claudia G. ^[2]

Afiliação do(s) autor(es)

^[1] Univ Aveiro, CICECO Aveiro Inst Mat, Dept Chem, P-3810193 Aveiro - Portugal

^[2] Univ Porto, Lab Separat & React Engn, Lab Catalysis & Mat LSRE LCM, Dept Chem Engn, Fac Engn, Rua Dr Roberto Frias, P-4200465 Porto - Portugal

^[3] Sao Paulo State Univ, Sch Pharmaceut Sci, Dept Engn Bioproc & Biotechnol, UNESP, Araraquara, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: SCIENTIFIC REPORTS; v. 11, n. 1 NOV 2 2021.
• Citações Web of Science: 0

Resumo

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 x 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. (AU)

• Processo FAPESP: 18/06908-8 - Desenvolvimento de nanomateriais sustentáveis para a purificação de fármacos antileucêmicos
• Beneficiário: Valéria de Carvalho Santos Ebinuma
• Modalidade de apoio: Auxílio à Pesquisa - Regular