EC Number   |
General Stability |
Reference |
|---|
    4.2.1.84 | active in acrylamide up to 60% w/v |
664408 |
| 4.2.1.84 | completely stabilized by 22 mM n-butyric acid |
648440 |
| 4.2.1.84 | Escherichia coli chaperones GroEL-ES work well in Rhodococcus and simultaneously possess protein-folding assistance functions and the ability to stabilize and reactivate the native nitrile hydratase |
748384 |
| 4.2.1.84 | immobilization and stabilization of a nitrile hydratase in the form of a cross-linked enzyme aggregate using ammonium sulfate as an aggregation agent followed by cross-linking with glutaraldehyde, method development and evaluation, overview. The stability of aggregated and immobilized enzyme is increased compared to enzyme in cell extract or whole cells |
698138 |
| 4.2.1.84 | KH2PO4-NaOH and Tris-HCl buffer are tested at 28°C and pH 7.5. 20% NHase activity is lost after 18 h and is further decreasing. 73.5 h later, NHase activity in Tris-HCl is unchanged while in KH2PO4-NaOH abrupt decrease is observed. |
671402 |
| 4.2.1.84 | loss of activity caused by storage at 0°C can be restored by irradiation with light of 370 nm |
648424 |
| 4.2.1.84 | nitrile hydratase cross-linked enzyme aggregates are sensitive to water-immiscible organic solvents as well as to aldehydes and hydrogen cyanide, but are remarkably stable and show useful activity in acidic aqueous environments of pH 4-5 |
701585 |
| 4.2.1.84 | organic acids stabilize, stable for more than 1 month in 0.1 M HEPES/KOH, pH 7.2, with 44 mM n-butyric acid, n-valeric acid, isovaleric acid, isobutyric acid or n-caproic acid |
648439 |
| 4.2.1.84 | potassium phosphate buffer has a negative effect on stability |
648422 |
| 4.2.1.84 | purified mutant NHases are stored in the dark without n-butyric acid, before use, NHases are activated by light irradiation. |
672689 |
