Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
diagnostics
-
the enzyme is a marker of chemotherapy dose modification during the induction phase in children with acute lymphoblastic leukemia, overview
analysis
-
direct measurement of L-asparagine in human plasma samples through the use of Escherichia coli Lasparaginase in the soluble form is a major clinical application of this system
analysis
-
biosensor for asparagine using a thermostable recombinant asparaginase from Archaeoglobus fulgidus immobilized in front of an ammonium-selective electrode. The biosensor has a detection limit of 0.06 mM for L-asparagine. It shows high stability
analysis
-
assembly a microplate-based biosensor for the determination of L-asparagine in biological samples. The enzyme is immobilized by crosslinking with glutaraldehyde in a microplate in 96-well format. The sensing is based on the colorimetric measurement of ammonia formation using the Nessler's reagent. The sensor enables monitoring of L-asparagine levels in serum and foods samples in the concentration range 10-200 microM, with a detection limit of 10 microM for L-asparagine
analysis
-
method based on IR spectroscopy to determine PEG-chitosan copolymer composition as well as composition of copolymer-enzyme conjugates. The method is reagentx02free and allows fast and reliable determination of parameters
biotechnology
-
development of a MCE method (micellar electrokinetic electrophoresis) that is sufficiently sensitive and selective for the separation of amino amides and determination of enzyme kinetic constants of L-Asnase
biotechnology
-
statistically based experimental design to maximize the production of glutaminase-free L-asparaginase. The individual optimum levels of initial pH of the medium, temperature, rpm of shaking incubator, and inoculum size are found to be 6.90, 29.8°C, 157 rpm, and 2.61% (v/v), respectively, for the production of L-asparaginase. After physical process parameters optimization, the production and productivity of L-asparaginase is enhanced by 26.39% (specific activity) and 10.19%, respectively. Maximization of L-asparaginase production is achieved at 12 h under optimal levels of physical process parameters in shake flask level
food industry
reduction of acrylamide level in biscuits and bread
food industry
the acrylamide contents in baked dough were reduced to sixty percent after treatment with recombinant enzyme as compared to the untreated control
food industry
-
the enzyme is used for reducing acrylamide formation during the potato frying process
food industry
-
the enzyme reduces acrylamide content in starchy fried food commodities
food industry
the final level of acrylamide in biscuits and bread is decreased by about 81.6% and 94.2%, respectively, upon treatment with 10 U asnase per mg flour
food industry
-
addition of partially purified L-asparaginase to potato products followed by incubation of the mixture at 37°C for 30 min leads to 92% reduction of acrylamide content
food industry
-
approximately 88.5% (0.978 mg/kg) acrylamide can be removed from fried potato chips by mutant V26A/E30G/D181G/V245G/G276D pre-treatment
food industry
pretreatment of potato chips and mooncakes with Asnase significantly decreases their acrylamide by 86% and 52%, respectively
food industry
-
the enzyme is used for reducing acrylamide formation during the potato frying process
-
food industry
-
reduction of acrylamide level in biscuits and bread
-
food industry
-
approximately 88.5% (0.978 mg/kg) acrylamide can be removed from fried potato chips by mutant V26A/E30G/D181G/V245G/G276D pre-treatment
-
medicine
-
enzyme has antitumor activity
medicine
-
enzyme has antitumor activity
medicine
-
enzyme has antitumor activity
medicine
-
enzyme has antitumor activity
medicine
-
enzyme has antitumor activity
medicine
Erwinia aroidea
-
enzyme has antitumor activity
medicine
-
enzyme is used in the treatment of acute lymphomic leukemia
medicine
-
a prospective therapeutic enzyme for leukemia treatment
medicine
-
the use of asparaginase II as a drug for the treatment of acute lymphoblastic leukemia is complicated by the significant glutaminase side activity of the enzyme. Selective reduction in glutaminase activity in variant B248A and other N248 variants
medicine
-
potent antineoplastic agent in animals which has given complete remission in some human leukemias
medicine
-
used for treatment of acute lymphoblastic leukemia, pancreatic carcinoma, and bovine lymphosarcoma
medicine
-
L-asparaginase is an anti-leukemic enzyme
medicine
-
L-asparaginase is important in the induction regimen for treating human acute lymphoblastic leukemia, cytotoxic complications are clinically significant problems lacking mechanistic insight, the enzyme is used in the treatment of both pediatric and adult forms of acute lymphoblastic leukemia, ALL
medicine
-
L-asparaginase is important in the induction regimen for treating human acute lymphoblastic leukemia, cytotoxic complications are clinically significant problems lacking mechanistic insight, the enzyme is used in the treatment of both pediatric andadult forms of acute lymphoblastic leukemia, ALL
medicine
-
the enzyme is a potential therapeutic agent in acute lymphocytic leukemia, acute lymphoblastic leukemia, and chromic myelogenyous leukemia, but causes high allergic reactions
medicine
-
the enzyme is used as therapeutic agent in the treatment of acute childhood lymphoblastic leukemia
medicine
-
the enzyme is used for acute lymphoblastic leukemia treatment, the enzyme does not reduces alpha-antiplasmin and plasminogen levels in human patients, overview
medicine
-
the enzyme is used for acute lymphoblastic leukemia treatment, the enzyme reduces alpha-antiplasmin and plasminogen levels in human patients, this together with the elevated level of thrombin activity in the patients lead to an enhanced risk for thrombosis due to delay in fibrin elimination in Escherichia coli L-asparaginase-treated patients, overview
medicine
-
the enzyme is widely used in chemotherapy for treatment of children with acute lymphoblastic leukemia, in vivo and in vitro resistance of the cells to the enzyme can occur
medicine
-
asparaginase is used in the treatment of acute lymphoblastic leukemia. It depletes plasma asparagine and glutamine, killing leukemic lymphoblasts but also causing immunosuppression. Asparaginase reduces maturing populations of normal B and T cells in thymus, bone marrow, and spleen of mice. Oral consumption of alanyl-glutamine mitigates metabolic stress in spleen, supporting the peripheral immune system and cell-mediated immunity during asparaginase chemotherapy
medicine
-
L-asparaginase is an anticancer agent. Developing an asparaginase production process based on bran of Glycine max as a substrate in solid state fermentation is economically attractive as it is a cheap and readily available raw material in agriculture-based countries
medicine
the enzyme can be efficiently immobilized on epoxy-activated Sepharose CL-6B. The immobilized enzyme retains most of its activity (60%) and shows high stability at 4°C. The approach offers the possibility of designing an L-asparaginase from Erwinia chrysanthemi bioreactor that can be operated over a long period of time with high efficiency, which can be used in leukaemia therapy
medicine
-
the enzyme is important to the treatment of acute lymphoblastic leukemia. Intravenous PEG-asparaginase (L-asparaginase covalently linked to polyethylene glycol) will eliminate painful injection, and achieve rapid peak levels and asparagine depletion
medicine
chemotherapeutic agent
medicine
-
treatment of lymphoma
medicine
-
asparaginase is one of the important bioactive compounds, which have curative effects in cancer treatment
medicine
-
L-asparaginase II from Erwinia carotovora may represent an important alternative therapy in the treatment of acute childhood lymphoblastic leukaemia, despite its promising lower glutaminase activity than Escherichia coli and Erwinia chrysanthemi L-asparaginases II
medicine
-
the enzyme is an important biopharmaceutical product used in the treatment of acute lymphoblastic leukaemia
medicine
-
anticancer drug
medicine
the enzyme is an important drug in the treatment of childhood acute lymphoblastic leukemia
medicine
the recombinant enzyme potentiate a lectin's induction of leukemic K562 cell apoptosis
medicine
enzyme potentiates a lectin's induction of leukemic K562 cell apoptosis, allowing lowering of the drug dosage and shortening of the incubation time
medicine
-
covalent immobilization of enzyme on functionalized aluminium oxide nanoparticles (AONP) and titanium oxide nanoparticles (TONP) for anticancer therapy. The nano-bioconjugates are optimally active at pH 7.0 and 40°C. TONP-asparaginase activity is enhanced in the presence of NH4+ (160%) and Mn2+ (165%) while AONP-asparaginase bioconjugates show increased relative activity with ethyl acetate (142%) and toluene (160%). The nano-bioconjugates display good reusability and maintain over 90% average activity after nine successive cycles. Maximum cytotoxicity (61%) is noticed with AONP-asparaginase against human leukemia MOLT-4 cells. AONP-asparaginase shows better affinity to L-asparagine as compared to free enzyme
medicine
-
enzyme shows antitumor proterties with IC50 values 0.036 mg/ml for MCF-7 cells, 0.037 mM/ml for HCT-116 cells, 0.046 mg/ml for Hep-G2 cells, respectively
medicine
-
L-asparaginase may significantly alter the interactions between microvascular endothelial cells, colon cancer cells, and components, resulting in colon cancer cell injury
medicine
-
purified L-asparaginase does not show hemolysis effect on blood erythrocytes. Recombinant L-asparaginase retains 50% of its initial activity after 90 and 60 min incubation in serum and trypsin separately
medicine
recombinant enzyme is able to inhibit the proliferation of K-562 and Jurkat cell lines
medicine
the anticancer activity of purified asparaginase is comparable or higher than that of commercial Escherichia coli asparaginase. The purified enzyme induces apoptotic cell death in dose-dependent manner, probybly via activation of anintrinsic apoptotic pathway. The purified enzyme is nontoxic for human noncancerous FR-2 cells and human blood lymphocytes
medicine
-
the purified enzyme inhibits the growth of human cell lines Hep-G2, MCF-7 and PC-3 with IC50 values of 14 microg/ml, 12.5 microg/ml and 37 microg/ml, respectively
medicine
-
the purified enzyme shows cytotoxicity for the MOLT-4 leukemic cell lineage
medicine
-
enzyme has antitumor activity
-
medicine
-
the purified enzyme shows cytotoxicity for the MOLT-4 leukemic cell lineage
-
medicine
-
the enzyme can be efficiently immobilized on epoxy-activated Sepharose CL-6B. The immobilized enzyme retains most of its activity (60%) and shows high stability at 4°C. The approach offers the possibility of designing an L-asparaginase from Erwinia chrysanthemi bioreactor that can be operated over a long period of time with high efficiency, which can be used in leukaemia therapy
-
medicine
-
the enzyme is used as therapeutic agent in the treatment of acute childhood lymphoblastic leukemia
-
medicine
-
chemotherapeutic agent
-
medicine
-
the enzyme is an important biopharmaceutical product used in the treatment of acute lymphoblastic leukaemia
-
medicine
-
the recombinant enzyme potentiate a lectin's induction of leukemic K562 cell apoptosis
-
medicine
-
used for treatment of acute lymphoblastic leukemia, pancreatic carcinoma, and bovine lymphosarcoma
-
medicine
-
L-asparaginase may significantly alter the interactions between microvascular endothelial cells, colon cancer cells, and components, resulting in colon cancer cell injury
-
medicine
-
enzyme shows antitumor proterties with IC50 values 0.036 mg/ml for MCF-7 cells, 0.037 mM/ml for HCT-116 cells, 0.046 mg/ml for Hep-G2 cells, respectively
-
medicine
-
potent antineoplastic agent in animals which has given complete remission in some human leukemias
-
pharmacology
-
L-asparaginase is a cancer chemotherapeutically important enzyme
pharmacology
-
L-asparaginase is a cancer chemotherapeutically important enzyme
-
synthesis
-
production of L-asparaginase from Serratia marcescens SK-07 in a batch bioreactor. The optimal levels of L-asparagine, glucose, yeast extract and peptone are 0.93, 3.81, 3.65 and 1.47 g/l, respectively, and maximal L-asparaginase production of 25.02 U mg/1 can be obtained. L-asparagine is the most favourable carbon source for enhanced production of L-asparaginase
synthesis
-
conjugation of enzyme to PEG-chitosan and glycol-chitosan imoproves catalytic efficiency 3- to 6fold under physiological conditions and enhances its resistance to thermal inactivation
synthesis
optimization of production and process conditions for recombinant human enzyme. The maximum biomass yield of 6.7 g/l of enzyme is achieved with fed-batch fermentation. The refolding efficiency is optimal at pH 8.5 (84%) and temperature 25°C (86%)
synthesis
KC573069
production and optimization of growth conditions results in submerged fermentation in modified M9 medium with yeast extract and fructose as carbon and nitrogen sources, respectively, at pH 8.0, incubated for 120 h at 30°C
synthesis
recombinant asparaginase isozyme AnsB fused with the pelB signal sequence and a five aspartate tag is secreted efficiently into culture medium at 34.6 U/mg cell of specific activity. By batch fermentation, recombinant Escherichia coli produces 40.8 U/ml asparaginase isozyme II in the medium. Deletion of the gspDE gene reduces extracellular production of asparaginase isozyme II
synthesis
-
strain is potent extracellular producer of L-asparaginase (347.42 IU) and shows 15fold enhancement of L-asparaginase production (5,205 U/gds) under submerged fermentation condition in 5 days in presence of inducers and activators. Red gram husk is the best substrate in solid state fermentation supporting maximum enzyme activity of 246.32 IU after 5 days of incubation
synthesis
-
strain is potent extracellular producer of L-asparaginase (347.42 IU) and shows 15fold enhancement of L-asparaginase production (5,205 U/gds) under submerged fermentation condition in 5 days in presence of inducers and activators. Red gram husk is the best substrate in solid state fermentation supporting maximum enzyme activity of 246.32 IU after 5 days of incubation
-
synthesis
-
production of L-asparaginase from Serratia marcescens SK-07 in a batch bioreactor. The optimal levels of L-asparagine, glucose, yeast extract and peptone are 0.93, 3.81, 3.65 and 1.47 g/l, respectively, and maximal L-asparaginase production of 25.02 U mg/1 can be obtained. L-asparagine is the most favourable carbon source for enhanced production of L-asparaginase
-
synthesis
-
production and optimization of growth conditions results in submerged fermentation in modified M9 medium with yeast extract and fructose as carbon and nitrogen sources, respectively, at pH 8.0, incubated for 120 h at 30°C
-