EC Number   |
Application |
Reference |
|---|
   4.3.1.1 | analysis |
scaled-down method for determination of aspartase activity in a 96-well microtitre plate |
715058 |
| 4.3.1.1 | biotechnology |
a complete biocatalytic process to synthesize high concentrations of L-aspartate catalyzed by aspartase from Bacillus sp. YM55-1 (AspB) is established using an immobilized enzyme in three different supports. MANA-agarose derivative could be selected as the most suitable biocatalyst for the synthesis of Asp due to the simplicity of the method and performance |
-, 729405 |
| 4.3.1.1 | biotechnology |
enhancement of recombinant protein production in Escherichia coli by coproduction of aspartase. The excretion of acetate by the aerobic growth of Escherichia coli on glucose is a manifestation of imbalanced flux between glycolysis and the tricarboxylic acid (TCA) cycle. This may restrict the production of recombinant proteins in E. coli, due to the limited amounts of precursor metabolites produced in TCA cycle. To approach this issue, an extra supply of intermediate metabolites in TCA cycle is made by conversion of aspartate to fumarate, a reaction mediated by the activity of L-aspartate ammonia-lyase |
665790 |
| 4.3.1.1 | biotechnology |
overview on commercial applications |
649266 |
| 4.3.1.1 | biotechnology |
putative and attractive enzyme for the enantioselective synthesis of N-substituted aspartic acids |
691802 |
| 4.3.1.1 | food industry |
propionic acid bacteria isolates originating from cheese show a wide range of aspartase activity. Aspartase activity is strain-dependent and each strain must be tested separately in order to be able to choose the most suitable starter culture for cheese production.70% of the 100 isolates tested, show very low levels of aspartate activity |
715058 |
| 4.3.1.1 | industry |
aspartate synthesis |
691570 |
| 4.3.1.1 | medicine |
involvement of enzyme in blood clotting and activation of plasminogen, overview |
649266 |
| 4.3.1.1 | synthesis |
bioproduction of L-aspartic acid and cinnamic acid. From an initial concentration of 1000 mM of fumarate and 30 mM of L-phenylalanine, the enzyme converts 0.395 mM L-aspartic acid and 3.47 mM cinnamic acid, respectively |
746796 |
| 4.3.1.1 | synthesis |
construction of hybrid enzyme from alpha-aspartyl dipeptidase and L-aspartase. The hybrid enzyme can be used in synthesis of the precursor for aspartame. Synthesizing aspartate from fumarate and NH4+, and then taking advantage of the catalytic action of alpha-aspartyl dipeptidase, the precursor of aspartame is produced |
663872 |
