13 documents found, page 1 of 2
One-step purification of L-asparaginase from cell extracts using carbon xerogels
Cristóvão, Raquel O.; Barros, Rita A. M.; Marramaque, Teresa P.; Aguiar, Gonçalo G.; Almeida, Mafalda R.; Carabineiro, Sónia A. C.L-asparaginase (ASNase, EC 3.5.1.1) is an enzyme with wide applications in the pharmaceutical sector and food processing industries. It is mainly used as a biotherapeutic for treating Acute Lymphoblastic Leukemia (ALL) and to reduce acrylamide formation in starchy compounds. Despite its relevance, current purification methods for microbial enzymes involve complex and expensive techniques. To overcome this drawb...
Recent developments and challenges in the application of fungal laccase for the...
Magalhães, Flávia F.; Pereira, Ana F. S.; Cristóvão, Raquel O.; Barros, Rita A. M.; Faria, Joaquim L.; Silva, Cláudia G.; Freire, Mara G.According to the European Environment Agency, the textile industry is responsible for 20% of global water pollution due to dyeing and finishing products, thus facing severe environmental challenges. It is essential to design more biocompatible and sustainable treatment processes capable of removing dyes from industrial wastewater to fight this environmental hazard. Chemical industries must change traditional ch...
Superior operational stability of immobilized l-asparaginase over surface-modif...
Almeida, Mafalda R.; Cristóvão, Raquel O.; Barros, Maria A.; Nunes, João C. F.; Boaventura, Rui A. R.; Loureiro, José M.; Faria, Joaquim L.Made available in DSpace on 2022-04-28T19:46:42Z (GMT). No. of bitstreams: 0 Previous issue date: 2021-12-01; Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP); Fundação para a Ciência e a Tecnologia; 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 d...
Carbon nanotubes for biomedical applications
Almeida, Mafalda R.; Nunes, João C. F.; Cristóvão, Raquel O.; Faria, Joaquim L.; Tavares, Ana P. M.; Silva, Cláudia G.; Freire, Mara G.Carbon nanotubes (CNTs) were discovered in 1991, and since then, have been one of the most intensely studied nanomaterials due to their improved functionalities and diversity of applications. Specifically, CNTs are entirely composed of carbon atoms connected through sp2 bonds structured in several condensed benzene rings rolled up into a cylinder form. Depending on the number of graphitic layers, CNTs can be cl...
Immobilization and characterization of l-asparaginase over carbon xerogels
Barros, Rita A. M.; Cristóvão, Raquel O.; Carabineiro, Sónia A. C.; Neves, Márcia C.; Freire, Mara G.; Faria, Joaquim L.; Santos-Ebinuma, Valéria C.L-asparaginase (ASNase) is an aminohydrolase currently used in the pharmaceutical and food industries. Enzyme immobilization is an exciting option for both applications, allowing for a more straightforward recovery and increased stability. High surface area and customizable porosity make carbon xerogels (CXs) promising materials for ASNase immobilization. This work describes the influence of contact time, pH, a...
Unveiling the Influence of Carbon Nanotube Diameter and Surface Modification on...
Cristóvão, Raquel O.; Barros, Rita A. M.; Pinho, João G.; Teixeira, Lília S.; Neves, Márcia C.; Freire, Mara G.; Faria, Joaquim L.L-asparaginase (ASNase, EC 3.5.1.1) is an amidohydrolase enzyme known for its anti-cancer properties, with an ever-increasing commercial value. Immobilization has been studied to improve the enzyme’s efficiency, enabling its recovery and reuse, enhancing its stability and half-life time. In this work, the effect of pH, contact time and enzyme concentration during the ASNase physical adsorption onto pristine and...
L-asparaginase-based biosensors
Nunes, João C. F.; Cristóvão, Raquel O.; Santos-Ebinuma, Valéria C.; Faria, Joaquim L.; Silva, Cláudia G.; Neves, Márcia C.; Freire, Mara G.L-asparaginase (ASNase) is an aminohydrolase enzyme widely used in the pharmaceutical and food industries. Although currently its main applications are focused on the treatment of lymphoproliferative disorders such as acute lymphoblastic leukemia (ALL) and acrylamide reduction in starch-rich foods cooked at temperatures above 100 ºC, its use as a biosensor in the detection and monitoring of L-asparagine levels ...
Superior operational stability of immobilized L-asparaginase over surface-modif...
Almeida, Mafalda R.; Cristóvão, Raquel O.; Barros, Maria A.; Nunes, João C. F.; Boaventura, Rui A. R.; Loureiro, José M.; Faria, Joaquim L.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 modifi...
Immobilization of L-asparaginase towards surface-modified carbon nanotubes
Tavares, Ana P. M.; Almeida, Mafalda R.; Cristóvão, Raquel O.; Barros, Maria A.; Nunes, João C. F.; Faria, Joaquim L.; Neves, Márcia C.; Freire, Mara G.L-asparaginase (LA) is an enzyme that catalyzes L-asparagine hydrolysis into L-aspartic acid and ammonia and is mainly applied in pharmaceutical and food industries. The LA 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-...
Immobilization of L-asparaginase towards surface-modified carbon nanotubes
Almeida, Mafalda R.; Cristóvão, Raquel O.; Barros, Maria A.; Nunes, João C.F.; Boaventura, Rui A. R.; Loureiro, José M.; Faria, Joaquim L.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, s...