Next Article in Journal
Strawberry Puree Functionalized with Natural Hydroxytyrosol: Effects on Vitamin C and Antioxidant Activity
Next Article in Special Issue
Room Temperature Ionic Liquids in Asymmetric Hetero-Ene Type Reactions: Improving Organocatalyst Performance at Lower Temperatures
Previous Article in Journal
Salvia officinalis L. from Italy: A Comparative Chemical and Biological Study of Its Essential Oil in the Mediterranean Context
Previous Article in Special Issue
More Efficient Prussian Blue Nanoparticles for an Improved Caesium Decontamination from Aqueous Solutions and Biological Fluids

Recent Strategies and Applications for l-Asparaginase Confinement

Laboratory of Separation and Reaction Engineering-Laboratory of Catalysis and Materials (LSRE-LCM), Department of Chemical Engineering, Faculty of Engineering, University of Porto, Rua do Dr. Roberto Frias, 4200-465 Porto, Portugal
Department of Chemistry, CICECO-Aveiro Institute of Materials, University of Aveiro, 3810-193 Aveiro, Portugal
School of Pharmaceutical Sciences, Universidade Estadual Paulista-UNESP, Araraquara 14800-903, Brazil
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Giancarlo Cravotto
Received: 2 November 2020 / Revised: 3 December 2020 / Accepted: 6 December 2020 / Published: 10 December 2020
l-asparaginase (ASNase, EC is an aminohydrolase enzyme with important uses in the therapeutic/pharmaceutical and food industries. Its main applications are as an anticancer drug, mostly for acute lymphoblastic leukaemia (ALL) treatment, and in acrylamide reduction when starch-rich foods are cooked at temperatures above 100 °C. Its use as a biosensor for asparagine in both industries has also been reported. However, there are certain challenges associated with ASNase applications. Depending on the ASNase source, the major challenges of its pharmaceutical application are the hypersensitivity reactions that it causes in ALL patients and its short half-life and fast plasma clearance in the blood system by native proteases. In addition, ASNase is generally unstable and it is a thermolabile enzyme, which also hinders its application in the food sector. These drawbacks have been overcome by the ASNase confinement in different (nano)materials through distinct techniques, such as physical adsorption, covalent attachment and entrapment. Overall, this review describes the most recent strategies reported for ASNase confinement in numerous (nano)materials, highlighting its improved properties, especially specificity, half-life enhancement and thermal and operational stability improvement, allowing its reuse, increased proteolysis resistance and immunogenicity elimination. The most recent applications of confined ASNase in nanomaterials are reviewed for the first time, simultaneously providing prospects in the described fields of application. View Full-Text
Keywords: l-asparaginase; confinement strategies; nanomaterials; therapeutic agents; acrylamide mitigation; biosensors l-asparaginase; confinement strategies; nanomaterials; therapeutic agents; acrylamide mitigation; biosensors
Show Figures

Graphical abstract

MDPI and ACS Style

Nunes, J.C.F.; Cristóvão, R.O.; Freire, M.G.; Santos-Ebinuma, V.C.; Faria, J.L.; Silva, C.G.; Tavares, A.P.M. Recent Strategies and Applications for l-Asparaginase Confinement. Molecules 2020, 25, 5827.

AMA Style

Nunes JCF, Cristóvão RO, Freire MG, Santos-Ebinuma VC, Faria JL, Silva CG, Tavares APM. Recent Strategies and Applications for l-Asparaginase Confinement. Molecules. 2020; 25(24):5827.

Chicago/Turabian Style

Nunes, João C.F., Raquel O. Cristóvão, Mara G. Freire, Valéria C. Santos-Ebinuma, Joaquim L. Faria, Cláudia G. Silva, and Ana P.M. Tavares 2020. "Recent Strategies and Applications for l-Asparaginase Confinement" Molecules 25, no. 24: 5827.

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop