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Results 1 - 10 of 57 > >>
EC Number Application Commentary Reference
Show all pathways known for 3.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.1analysis 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 753459
Show all pathways known for 3.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.1analysis 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 723942
Show all pathways known for 3.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.1analysis 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 686239
Show all pathways known for 3.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.1analysis 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 752737
Show all pathways known for 3.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.1biotechnology 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 711845
Show all pathways known for 3.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.1biotechnology 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 710917
Show all pathways known for 3.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.1diagnostics the enzyme is a marker of chemotherapy dose modification during the induction phase in children with acute lymphoblastic leukemia, overview 668132
Show all pathways known for 3.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.1food 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 753361
Show all pathways known for 3.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.1food 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 -, 754219
Show all pathways known for 3.5.1.1Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.1food industry pretreatment of potato chips and mooncakes with Asnase significantly decreases their acrylamide by 86% and 52%, respectively 753874
Results 1 - 10 of 57 > >>