EC Number |
General Stability |
Reference |
---|
1.1.3.4 | 3°C, little loss of activity, 3 years |
389805 |
1.1.3.4 | 4.0 M urea, immunoaffinity-layered preparation retains 87% of original activity after 2 h and 40% of activity after 24 h of incubation, whereas the soluble enzyme loses all of its activity within 1 h of preincubation |
655079 |
1.1.3.4 | after immobilization of the oxidized GOX with silver nanoparticles, the Km and Vmax of the immobilization enzyme remarkably reduce and increase, respectively. While the bioconjugate is stable in lower temperatures and also in neutral to basic pH, the enzymatic activity of the bioconjugate slightly decreases in higher temperature |
710858 |
1.1.3.4 | Ca2+ and Mg2+ at 1 M induce compaction of the native conformation of the enzyme, and the enzyme shows a higher stability as compared to the native enzyme against urea denaturation, Ca2+ and Mg2+ at concentrations above 2 M induce dissociation of the native dimeric enzyme, resulting in stabilization of the enzyme monomer, 3 M Ca2+-stabilized monomer retains about 70% secondary structure present in the native enzyme dimer, however there is a complete loss of cooperative interactions between these secondary structural elements present in the enzyme |
389837 |
1.1.3.4 | chemical denaturation by 6.67 M guanidine HCl is accompanied by dissociation of the homodimeric enzyme into monomers |
656254 |
1.1.3.4 | comparative stability of insoluble complexes of enzyme obtained with concanavalin A and glycosyl-specific polyclonal antibodies, overview |
677260 |
1.1.3.4 | comparison of stability immobilized on various materials |
389804 |
1.1.3.4 | D2O stabilizes |
389790 |
1.1.3.4 | divalent cations such as Ba2+, Ca2+ and Mg2+ have a slightly negative effect on stability |
389790 |
1.1.3.4 | encapsulation of the enzyme in the liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine increases the enzyme stability through its decreased inhibition because of H2O2 produced in glucose oxidation |
654909 |