EC Number   |
General Stability |
Reference |
|---|
   3.5.5.1 | efficient biocatalyst recycling is achieved as a result of immobilization with immobilized cells exhibiting 88% conversion even after 20 batch recycles |
667290 |
| 3.5.5.1 | for immobilization of cells with nitrilase activity a variety of sol-gel silica hybrids are tested for entrapment and adsorption of bacterial cells as well as chemical binding on polysulphone membranes. Activation of the matrix surface with formaldehyde leads to an increase in immobilization efficiency and operational stability of the biocatalyst. Among the supports screened, membranes give the best result for enzyme activity and especially operational stability, with retention of 100% activity after eight reaction cycles |
669740 |
| 3.5.5.1 | high recycling efficiency of enzyme ecapsulated in ethyleneamine-mediated biosilica. The residual activity of the enzyme ecapsulated in ethyleneamine-mediated biosilica retains 94.2% of its initial activity after 16 cycles of reaction. Even after 20 cycles, its residual activity keeps approximately 77.1% of its initial activity |
756955 |
| 3.5.5.1 | highly unstable, complete loss of activity on freezing |
209763 |
| 3.5.5.1 | maximal nitrilase activity of alginate-immobilized cells is obtained under conditions of 2% (w/v) alginate, 0.6% (w/v) CaCl2, 0.4 g cell/g alginate, and 1.8 mm bead size |
733521 |
| 3.5.5.1 | more resistant to thermal inactivation if cells immobilized in calcium alginate beads, stabilizing effect of 3-cyanopyridine |
209745 |
| 3.5.5.1 | nitrilase aggregates are prepared using ammonium sulfate (35%) precipitation followed by cross-linking with glutaraldehyde (125 mM) which renders 70% activity retention |
711496 |
| 3.5.5.1 | the enzyme ecapsulated in ethyleneamine-mediated biosilica has significantly improved temperature tolerance |
756955 |
| 3.5.5.1 | the enzyme stability is markedly improved in the presence of D-sorbitol and xylitol (20% w/v), or myo-inositol (10% w/v) |
684594 |
| 3.5.5.1 | the nitrilase activity in cross-linked enzyme aggregates is at 30°C and 60°C about 5times more stable than in soluble preparations |
684250 |
