Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry
Applied Biochemistry and Biotechnology, 2021 L-glutaminases are enzymes that catalyze the hydrolysis of L-glutamine, producing L-glutamate and ammonium, and they have promising applications in pharmaceutical and food industries. Several investigations have focused on thermo-tolerant L-glutaminases; however, studies on cold-adapted L-glutaminases have not been reported.
Flavia V. Ferreira +5 more
openaire +3 more sources
L-Asparaginase from Penicillium sizovae Produced by a Recombinant Komagataella phaffii Strain
Pharmaceuticals, 2022 L-asparaginase is an important enzyme in the pharmaceutical field used as treatment for acute lymphoblastic leukemia due to its ability to hydrolyze L-asparagine, an essential amino acid synthesized by normal cells, but not by neoplastic cells.
Marcela Freitas +10 more
doaj +1 more source
A Novel L-Asparaginase from Enterobacter sp. Strain M55 from Maras Salterns in Peru [PDF]
Chemical and Biochemical Engineering Quarterly, 2022 L-Asparaginase (ASNase) is used in medicine for neoplasms treatment and in food industry for mitigation of acrylamide in high-temperature processed food.
A. Hurtado +8 more
doaj +1 more source
F1000Research, 2020 Background: The mangrove, Rhizophora mucronata, an essential source of endophytic bacteria, was investigated for its ability to produce glutaminase-free L-asparaginase.
Asep Awaludin Prihanto +3 more
doaj +1 more source
, 2019 After metabolic reprogramming, many cancer cells become glutamine addicted, that is, they depend on a high consumption of this amino acid for their survival and proliferation.
Campos-Sandoval, José A. +2 more
core +1 more source
Purification and properties of L-glutaminase-L-asparaginase from Pseudomonas acidovorans [PDF]
Journal of Bacteriology, 1977 An enzyme that catalyzes the hydrolysis of both glutamine and asparagine has been purified to homogeneity from extracts of Pseudomonas acidovorans. The enzyme having a ratio of glutaminase to asparaginase of 1.45:1.0 can be purified by a relatively simple procedure and is stable upon storage.
L, Davidson +4 more
openaire +2 more sources
Engineering of Helicobacter pylori L-asparaginase: characterization of two functionally distinct groups of mutants. [PDF]
PLoS ONE, 2015 Bacterial L-asparaginases have been used as anti-cancer drugs for over 4 decades though presenting, along with their therapeutic efficacy, several side effects due to their bacterial origin and, seemingly, to their secondary glutaminase activity ...
Maristella Maggi +3 more
doaj +1 more source
GLUTAMINASE FREE L-ASPARAGINASE PRODUCING ENDOPHYTES FROM MANGROVES [PDF]
, 2016 Objective: To screen endophytes isolated from mangroves for their potential to produce glutaminase free L-asparaginase .Methods: Endophytes were isolated from leaves and stems of three mangrove plants using surface sterilization technique followed by ...
G, Salini
core +1 more source
Optimised production of L-glutaminase: A tumour inhibitor from Aspergillus flavus cultured on agroindustrial residues [PDF]
, 2013 L-Glutaminase, an amidohydrolase enzyme has been a choice of interest in the treatment of lymphoblastic leukemia. This study investigates the production and optimization of extracellular glutaminase enzyme using several agro-industrial residues by ...
Nath, SS +3 more
core +1 more source
TNF-α promotes extracellular vesicle release in mouse astrocytes through glutaminase
Journal of Neuroinflammation, 2017 Background Extracellular vesicles (EVs) are membrane-contained vesicles shed from cells. EVs contain proteins, lipids, and nucleotides, all of which play important roles in intercellular communication.
Kaizhe Wang +6 more
doaj +1 more source