ArticleRSC advances2020
Development and characterization of a novel l-asparaginase/MWCNT nanobioconjugate.
Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 31 citations in OpenAlex.
- Graphitic Carbon Nitride: A Reusable and Stable Support for Glucose Oxidase.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- l-Asparaginase Immobilized on Nanographene Oxide as an Efficient Nanobiocatalytic Tool for Asparagine Depletion in Leukemia Cells.Bioconjugate chemistry · 2025Article
- Aliivibrio fischeri L-Asparaginase production by engineered Bacillus subtilis: a potential new biopharmaceutical.Bioprocess and biosystems engineering · 2022Article
- Immobilization and Characterization of L-Asparaginase over Carbon Xerogels.Biotech (Basel (Switzerland)) · 2022Article
- Enhanced Enzyme Reuse through the Bioconjugation of L-Asparaginase and Silica-Based Supported Ionic Liquid-like Phase Materials.Molecules (Basel, Switzerland) · 2022Article
- Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes.Scientific reports · 2021Article
- Expanding the bio-catalysis scope and applied perspectives of nanocarrier immobilized asparaginases.3 Biotech · 2021Review
- Recent Strategies and Applications for l-Asparaginase Confinement.Molecules (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.