2019
DOI: 10.1039/c8ra09244c
|View full text |Cite
|
Sign up to set email alerts
|

Immobilization adjusted clock reaction in the urea–urease–H+ reaction system

Abstract: The reported immobilization shifts the bell-shaped reactivity-pH curve to lower pHs and enables the clock reaction to occur from a very low initial pH, where the free enzyme had already lost its activity.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
6
0

Year Published

2020
2020
2024
2024

Publication Types

Select...
6

Relationship

2
4

Authors

Journals

citations
Cited by 17 publications
(14 citation statements)
references
References 27 publications
0
6
0
Order By: Relevance
“…As previously mentioned, Zn 2+ itself is a strong inhibitor for the enzyme, in addition to this, when the enzyme is embedded in the precipitate, the diffusion of the substrate towards the active sites is strongly hindered. The net result would be that the real concentration of reactive urea is much lower than the theoretical one, as it happens when urease is loaded on resin particles [12]. In amino resin particles, the bell shape is shifted to lower pH values and the stability of the enzyme is increased.…”
Section: Resultsmentioning
confidence: 95%
See 2 more Smart Citations
“…As previously mentioned, Zn 2+ itself is a strong inhibitor for the enzyme, in addition to this, when the enzyme is embedded in the precipitate, the diffusion of the substrate towards the active sites is strongly hindered. The net result would be that the real concentration of reactive urea is much lower than the theoretical one, as it happens when urease is loaded on resin particles [12]. In amino resin particles, the bell shape is shifted to lower pH values and the stability of the enzyme is increased.…”
Section: Resultsmentioning
confidence: 95%
“…1) and since stoichiometrically twice ammonia is produced than carbon dioxide, the pH continuously increases in an unbuffered medium [42]. In experiments, the initial pH of the reaction mixture was set to pH ~ 4 by acetic acid, and due to the bell-shaped activity dependence of the enzyme on pH (having a maximum at pH = 8.2 [12]) a sigmoidal kinetic curve (pH versus time) can be obtained. Figure 1a shows typical kinetic curves obtained in the urea-urease enzymatic reaction, it can be seen that the clock time ranges between ~ 30 and ~ 200 s in the excess substrate (urea) depending on the enzyme concentration.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Urease activity was quantified by measuring the O.D. at 530 nm using a UV–Visible spectrophotometer [ 35 ].…”
Section: Methodsmentioning
confidence: 99%
“…Therefore, the enzyme-immobilized associative polyelectrolyte has greater activity, reversibility, and stability. [11] Angewandte Chemie…”
Section: Angewandte Chemiementioning
confidence: 99%