The Effect of Ionic Strength on the Heat of Hydrolysis of Benzoyl-L-argininamide1

1956 ◽  
Vol 78 (7) ◽  
pp. 1349-1352 ◽  
Author(s):  
Waldie W. Forrest ◽  
Herbert Gutfreund ◽  
Julian M. Sturtevant
Keyword(s):  
Ionic Strength ◽  
Hydrolysis Of ◽  
Heat Of Hydrolysis

Kinetics of hydrolysis of peroxodisulphate ions in acidic medium to peroxomonosulphuric acid

1981 ◽  
Vol 46 (5) ◽  
pp. 1229-1236 ◽  
Author(s):  
Jan Balej ◽  
Milada Thumová
Keyword(s):  
Ionic Strength ◽  
Rate Constants ◽  
Acidic Medium ◽  
Measured Data ◽  
Molar Ratios ◽  
Starting Solution ◽  
Kinetics Of Hydrolysis ◽  
Rate Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of

The rate of hydrolysis of S2O82- ions in acidic medium to peroxomonosulphuric acid was measured at 20 and 30 °C. The composition of the starting solution corresponded to the anolyte flowing out from an electrolyser for production of this acid or its ammonium salt at various degrees of conversion and starting molar ratios of sulphuric acid to ammonium sulphate. The measured data served to calculate the rate constants at both temperatures on the basis of the earlier proposed mechanism of the hydrolysis, and their dependence on the ionic strength was studied.

Effect of Chloride Ions on the Hydrolysis of Trivalent Lanthanum, Praseodymium and Lutetium in Aqueous Solutions of 2 M Ionic Strength

2005 ◽  
Vol 34 (4) ◽  
pp. 427-441 ◽  
Author(s):  
H. López-González ◽  
M. Solache-Ríos ◽  
M. Jiménez-Reyes ◽  
J. J. Ramírez-García ◽  
A. Rojas-Hernández
Keyword(s):  
Ionic Strength ◽  
Aqueous Solutions ◽  
Chloride Ions ◽  
Hydrolysis Of

ÉTUDE DES EFFETS ÉLECTROSTATIQUES SUR LE MÉCANISME D'ACTION CATALYTIQUE DE LA PHOSPHATASE ALCALINE INTESTINALE DE VEAU

1965 ◽  
Vol 43 (8) ◽  
pp. 2222-2235 ◽  
Author(s):  
Michel Lazdunski ◽  
Jacques Brouillard ◽  
Ludovic Ouellet
Keyword(s):  
Dielectric Constant ◽  
Ionic Strength ◽  
Maximum Activity ◽  
Enzyme Molecule ◽  
High Substrate Concentration ◽  
Nitrophenyl Phosphate ◽  
Phosphatase Alcaline ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of ◽  
Activated Complex

The influence of dioxane and ethanol on the rate of hydrolysis of p-nitrophenyl phosphate in the presence of an intestinal alcaline phosphatase can be interpreted as a dielectric constant effect, at high substrate concentration. The dielectric constant effect is a function of the pH of the medium and is maximum around pH 9.4 at 25 °C and pH 9.0 at 15 °C. An interpretation suggesting that the change in diameter of the enzyme molecule becoming an activated complex is minimum at a pH of maximum activity is proposed. The same model can take into account the influence of the ionic strength on the same reaction.

The heat of hydrolysis of boron tribromide

1955 ◽  
Vol 51 ◽  
pp. 19 ◽  
Author(s):  
H. A. Skinner ◽  
N. B. Smith
Keyword(s):  
Boron Tribromide ◽  
Hydrolysis Of ◽  
Heat Of Hydrolysis

scholarly journals Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions

1993 ◽  
Vol 289 (3) ◽  
pp. 897-902 ◽  
Author(s):  
M Mossakowska ◽  
J Moraczewska ◽  
S Khaitlina ◽  
H Strzelecka-Golaszewska
Keyword(s):  
Electron Microscopy ◽  
Steady State ◽  
Ionic Strength ◽  
Rate Constants ◽  
Initial Rate ◽  
Critical Concentration ◽  
Rate Of Polymerization ◽  
Low Ionic Strength ◽  
Hydrolysis Of

Homogeneous preparations of actin devoid of the three C-terminal residues were obtained by digestion of G-actin with trypsin after blocking proteolysis at other sites by substitution of Mg2+ for the tightly bound Ca2+. Removal of the C-terminal residues resulted in the following: an enhancement of the Mg(2+)-induced hydrolysis of ATP in low-ionic-strength solutions of actin; an increase in the critical concentration for polymerization; a decrease in the initial rate of polymerization; and an enhancement of the steady-state exchange of subunits in the polymer. Electron microscopy indicated an increased fragility of the filaments assembled from truncated actin. The results suggest that removal of the C-terminal residues increases the rate constants for monomer dissociation from the polymer ends and from the oligomeric species.

Mechanistic Information from the Effect of Pressure on the Kinetics of Hydrolysis of Iodopentaaquochromium(III) Ion

1975 ◽  
Vol 53 (24) ◽  
pp. 3697-3701 ◽  
Author(s):  
Milton Cornelius Weekes ◽  
Thomas Wilson Swaddle
Keyword(s):  
Ionic Strength ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Hydrogen Ion Concentration ◽  
Kinetics Of Hydrolysis ◽  
Rate Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Aqueous Hclo ◽  
Conjugate Base

The rate of hydrolysis of iodopentaaquochromium(III) ion has been measured as a function of pressure (0.1 to 250 MPa) and hydrogen ion concentration (0.1 to 1.0 mol kg−1) at 298.2 K and ionic strength 1.0 mol kg−1 (aqueous HClO4–LiClO4). The volumes of activation for the acid independent and inversely acid dependent hydrolysis pathways are −5.4 ± 0.5 and −1.6 ± 0.3 cm3 mol−1 respectively, and are not detectably pressure-dependent. Consideration of these values, together with the molar volume change of −3.3 ± 0.3 cm3 mol−1 determined dilatometrically for the completed hydrolysis reaction, indicates that the mechanisms of the two pathways are associative interchange (Ia) and dissociative conjugate base (Dcb) respectively.

scholarly journals A Study on the Hydrolysis of Urea Contained in Wastewater and Continuous Recovery of Ammonia by an Enzymatic Membrane Reactor

Processes ◽  
2021 ◽  
Vol 9 (10) ◽  
pp. 1703
Author(s):  
Mukhtar Nuhu Yahya ◽  
Hüseyin Gökçekuş ◽  
Derin Orhon ◽  
Bülent Keskinler ◽  
Ahmet Karagunduz ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Enzymatic Hydrolysis ◽  
Membrane Reactor ◽  
Ammonium Nitrogen ◽  
Feed Concentration ◽  
Filtration Membrane ◽  
Urease Enzyme ◽  
Ultra Filtration ◽  
Hydrolysis Of ◽  
Hydrolysis Of Urea

1. Background: Urea is the main product of the nitrogenous breakdown of protein metabolism in mammals. In this study, process intensification for enzymatic hydrolysis of urea by urease enzyme (jack bean urease) was examined in a membrane reactor. 2. Methods: Batch and continuous enzymatic hydrolysis reactions were performed at different substrate concentrations to determine the digestibility and affinity of the substrate with that of the enzyme. The hydrolysate samples were obtained by an optimized continuous enzyme membrane reactor (EMR) coupled with an ultra-filtration membrane (250 kDa). Feed concentration varied from 100 to 500 mg/L. Laboratory experiments were conducted at room temperature (20 ± 1 °C), with a flow rate of 20 mL/min, urease concentration of 0.067 g/L, ionic strength (I = 0, 0.01, 0.05), and ammonium nitrogen addition of (0, 100 mg/L, 200 mg/L, 500 mg/L). Moreover, the effect of ionic strength, ammonium nitrogen concentration, feed concentration, and enzyme concentration on urea hydrolysis was examined. Scanning electron microscopy (SEM) and energy dispersive X-ray spectroscopy (EDAX) analysis were used to identify the physicochemical properties as well as the elemental composition of the Ultra-Filtration membrane used in this study. 3. Results: The study revealed that higher ionic strength and higher concentrations of NH4SO2 and ammonium nitrogen (NH3-N) inhibithydrolysis of urea by reducing the urease enzyme activity in the system over time. 4. Conclusions: Herein, a sustainable alternative for the conversion of urea to ammonia by utilizing urease in an EMR was demonstrated.

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