Kinetic Studies on Oxidation of Veratryl Alcohol by Laccase-Mediator System. Part 1. Effects of Mediator Concentration

Holzforschung ◽  
2000 ◽  
Vol 54 (2) ◽  
pp. 165-170 ◽  
Author(s):  
Mikhail Yu. Balakshin ◽  
Chen-Loung Chen ◽  
Josef S. Gratzl ◽  
Adrianna G. Kirkman ◽  
Harald Jakob
Keyword(s):  
Kinetic Studies ◽  
Veratryl Alcohol ◽  
Alcohol Oxidation ◽  
Order Rate Constant ◽  
Molar Ratio ◽  
Active Centers ◽  
First Order ◽  
System Part ◽  
Kinetics Of

Summary Kinetics of the laccase-catalyzed oxidation of veratryl alcohol with dioxygen in the presence of 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diamonium salt (ABTS), the mediator, were studied to elucidate the possible reaction mechanism and the role of the mediator in this reaction. The reaction follows a pseudo-first order reaction law. The first order rate constant (κ) is dependent on the Mediator/Substrate (M/S) ratio and has a maximum at M/S molar ratio of 0.15. The kinetic studies show that the mechanism of veratryl alcohol oxidation with dioxygen-laccase-ABTS is rather complex and includes different reaction pathways. The mediator is involved in competitive reactions. It has been suggested that at low mediator concentration, the veratryl alcohol is oxidized via the laccase redox cycle. The mediator acts mostly as a laccase activator at a M/S ratio lower than 0.15. With increasing ABTS concentration with respect to the substrate concentration, ABTS acts increasingly as a cosubstrate competing with the original substrate for active centers of the laccase. This results in inhibition of veratryl alcohol oxidation in the enzyme cycle and increases the role of substrate oxidation by an oxidized mediator.

Kinetics of bioactive compounds in functional spice Jiangpo during thermal processing

2012 ◽  
Vol 8 (3) ◽  
Author(s):  
Xiaoyan Dai ◽  
Chenhuan Yu ◽  
Qiaofeng Wu
Keyword(s):  
Kinetic Parameters ◽  
Bioactive Compounds ◽  
Thermal Processing ◽  
Order Rate Constant ◽  
Heat Processing ◽  
Order Kinetic ◽  
Time Intervals ◽  
First Order ◽  
Order Kinetic Model ◽  
Kinetics Of

Abstract Jiangpo is an increasingly popular East Asian spice which is made from Mangnolia officinalis bark and ginger juice. Since it induces bioactive compounds decomposition and has influence on final flavor and fragrance, cooking is regarded as the key operation in preparation of Jiangpo. To evaluate the bioactive compounds content changes of Jiangpo during thermal processing, kinetic parameters including reaction order, rate constant, T1/2 and activation energy of bioactive markers namely honokiol, magnolol and curcumin were determined. Cooking was set at temperatures 60, 90 and 120 °C for selected time intervals. Results displayed the thermal kinetic characteristics of the three compounds. Thermal degradation of Honokiol and magnolol both followed first order kinetic model and the loss of curcumin fitted second order. A mathematical model based on the obtained kinetic parameters has also been developed to predict the degradation of honokiol, magnolol and curcumin in non-isothermal state. All the information in this paper could contribute necessary information for optimizing the existing heat processing of Jiangpo.

scholarly journals Kinetics of K release from soils of Brazilian coffee regions: effect of organic acids

2008 ◽  
Vol 32 (2) ◽  
pp. 533-540 ◽  
Author(s):  
Vladimir Antônio Silva ◽  
Giuliano Marchi ◽  
Luiz Roberto Guimarães Guilherme ◽  
José Maria de Lima ◽  
Francisco Dias Nogueira ◽  
...  
Keyword(s):  
Release Kinetics ◽  
Kinetic Studies ◽  
Release Rates ◽  
First Order ◽  
Potassium Release ◽  
Minas Gerais State ◽  
Soil Clay ◽  
Extractant Solution ◽  
Kinetics Of ◽  
K Release

Kinetic studies on soil potassium release can contribute to a better understanding of K availability to plants. This study was conducted to evaluate K release rates from the whole soil, clay, silt, and sand fractions of B-horizon samples of a basalt-derived Oxisol and a sienite-derived Ultisol, both representative soils from coffee regions of Minas Gerais State, Brazil. Potassium was extracted from each fraction after eight different shaking time periods (0-665 h) with either 0.001 mol L-1 citrate or oxalate at a 1:10 solid:solution ratio. First-order, Elovich, zero-order, and parabolic diffusion equations were used to parameterize the time dependence of K release. For the Oxisol, the first-order equation fitted best to the experimental data of K release, with similar rates for all fractions and independent of the presence of citrate or oxalate in the extractant solution. For all studied Ultisol fractions, in which K release rates increased when extractions were performed with citrate solution, the Elovich model described K release kinetics most adequately. The highest potassium release rate of the Ultisol silt fraction was probably due to the transference of "non-exchangeable" K to the extractant solution, whereas in the Oxisol exchangeable potassium represented the main K source in all studied fractions.

Oxidation of Nickel(II) and Manganese(II) by Peroxodisulfate in Aqueous Solution in the Presence of Molybdate. Crystal Structure of the (NH4)6[NiMo9O32].6H2O Product

1992 ◽  
Vol 45 (12) ◽  
pp. 1943 ◽  
Author(s):  
SJ Dunne ◽  
RC Burns ◽  
GA Lawrance
Keyword(s):  
Rate Constant ◽  
Linear Dependence ◽  
Ph Dependence ◽  
Order Rate Constant ◽  
X Ray Diffraction ◽  
X Ray ◽  
First Order ◽  
Oxidant Concentration ◽  
Ph Range ◽  
Kinetics Of

Oxidation of Ni2+,aq, by S2O82- to nickel(IV) in the presence of molybdate ion, as in the analogous manganese system, involves the formation of the soluble heteropolymolybdate anion [MMogO32]2- (M = Ni, Mn ). The nickel(IV) product crystallized as (NH4)6 [NiMogO32].6H2O from the reaction mixture in the rhombohedra1 space group R3, a 15.922(1), c 12.406(1) � ; the structure was determined by X-ray diffraction methods, and refined to a residual of 0.025 for 1741 independent 'observed' reflections. The kinetics of the oxidation were examined at 80 C over the pH range 3.0-5.2; a linear dependence on [S2O82-] and a non-linear dependence on l/[H+] were observed. The influence of variation of the Ni/Mo ratio between 1:10 and 1:25 on the observed rate constant was very small at pH 4.5, a result supporting the view that the precursor exists as the known [NiMo6O24H6]4- or a close analogue in solution. The pH dependence of the observed rate constant at a fixed oxidant concentration (0.025 mol dm-3) fits dequately to the expression kobs = kH [H+]/(Ka+[H+]) where kH = 0.0013 dm3 mol-1 s-1 and Ka = 4-0x10-5. The first-order dependence on peroxodisulfate subsequently yields a second-order rate constant of 0.042 dm3 mol-1 s-1. Under analogous conditions, oxidation of manganese(II) occurs eightfold more slowly than oxidation of nickel(II), whereas oxidation of manganese(II) by peroxomonosulfuric acid is 16-fold faster than oxidation by peroxodisulfate under similar conditions.

scholarly journals Compounds of 6, 13-Diamino-6, 13-Dimethyl-1, 4, 8, 11 - Tetraazacyclotetradecane

2021 ◽  
Author(s):  
◽  
Asokamali Siriwardena
Keyword(s):  
Rate Constants ◽  
Magnetic Measurements ◽  
Order Rate Constant ◽  
Acidic Solutions ◽  
First Order ◽  
Order Rate ◽  
Pendant Arm ◽  
Nickel Copper ◽  
13C Nuclear Magnetic Resonance ◽  
Kinetics Of

<p>The reaction of bis-(diaminoethane)nickel(II) chloride, ([Ni(en)2]Cl2 in methanol with formaldehyde and nitroethane in the presence of triethylamine proceeds readily to produce (6, 13-dimethyl-6, 13-dinitro-1, 4, 8, 11-tetraazacyclotetradecane)nickel(II) chloride, [Ni(dini)] - Cl2. Reduction of the nitro groups of this compound by catalytic hydrogenation yields three isomers of the pendant arm macrocyclic complex (6, 13-diamino-6, 13-dimethyl-1, 4, 8, 11-tetraazachyclotetradecane)nickel(II) chloride, designated a-, b- and c-[Ni(diam)]Cl2. These were separated by fractional crystallization. The aisomer was observed to isomerizes slowly in solution to the b- form. A parallel dissociation reaction of the a- isomer was also observed. The demetallation of a- and b- isomers of the diam complex of nickel by reaction with cyanide or concentrated acid at 140 degrees C produces the macrocycle meso-(6, 13-diamino-6, 13-dimethyl-1, 4, 8, 11-tetraazacyclotetra-decane), diam. A variety of hexamine, pentamine and tetramine complexes of diam with nickel(II), copper(II), cobalt(II) and (III), chromium(III), palladium(II), rhodium(III), zinc(II) and cadmium(II) were prepared. Hexamine and tetramine forms of labile metal complexes could be rapidly and reversibly interconverted by altering the pH. The hexamine cobalt(III) cation, [Co(diam)]3+ was by far the most inert of the prepared cobalt(III) complexes, remaining unaffected in hot acidic solutions. In contrast, a single pendant arm of the hexamine [Cr(diam)]3+ cation could be dissociated in acid. (Two possibly triamine complexes of lead were also prepared). These compounds were characterized by elemental analysis, magnetic measurements, electronic, infrared, 1H and 13C nuclear magnetic resonance spectra. The pendant arm protonation constants (log K) of diam and selected complexes of nickel, copper and palladium were calculated from potentiometric titration measurements at 25 degrees C. The log K values for diam at 25 degrees C (I = 0.1 M NaclO4) were 11.15, 9.7, 6.2 and 5.3. Kinetics of the parallel isomerization and dissociation of a-[Ni(dimH2)]4+ in HCl/NaCl solutions were monitored spectrophotometrically at 50 degrees C. The rate of reaction in acidic solutions showed a non-linear dependency on acid concentration. The observed first order rate constant (kobs) for disappearance of a-[Ni(diamH2)]4+ (by isomerization and dissociation) in 2.0 M HCl, 0.1 M NaOH and 2.0 M NaCl were 3.05 x 10-4, 2.0(3) x 10-2 and 5.0 x 10-5 s-1 respectively. The rate of the dissociation component of the reaction of a-[Ni(diamH2)]4+ in 2.0 M HCl at 50 degrees C was 1.82 x 10-7 s-1. Acid bydrolysis kinetics of (Cu[diamH2])(ClO4)4 in hydrochloric acid and perchloric acid at 50 and 70 degrees C were studied spectrophotometrically. The reactions were slow and the observed first order rate constants were to a first approximation independent of the particular acid or its concentration. The observed first order rate constants were 1 x 10-9 and 8 x 10-9 s-1 at 50 and 70 degrees C respectively. Questions about the nature of the reaction being followed have been raised.</p>

Kinetics of Plasmon-Driven Hydrosilylation of Silicon Surfaces: Photogenerated Charges Drive Silicon- Carbon Bond Formation

2021 ◽  
Author(s):  
Chengcheng Rao ◽  
Brian Olsen ◽  
Erik Luber ◽  
Jillian Buriak
Keyword(s):  
Green Light ◽  
Kinetic Studies ◽  
Silicon Surfaces ◽  
Moderate Intensity ◽  
Carbon Bond ◽  
Silicon Carbon ◽  
Set Up ◽  
Kinetics Of ◽  
Insight Into

Optically transparent PDMS stamps coated with a layer of gold nanoparticles were employed as plasmonic stamps to drive surface chemistry on silicon surfaces. Illumination of a sandwich of plasmonic stamps, an alkene ink, and hydride-terminated silicon with green light of moderate intensity drives hydrosilylation on the surface. The key to the mechanism of the hydrosilylation is the presence of holes at the Si-H-terminated interface, which is followed by attack by a proximal alkene and formation of the silicon-carbon bond. In this work, detailed kinetic studies of the hydrosilylation on silicon with different doping levels, n++, p++, n, p, and intrinsic were carried out to provide further insight into the role of the metal-insulator-semiconductor (MIS) junction that is set up during the stamping.

Kinetics of reconstitution of apotyrosinase by copper

1990 ◽  
Vol 68 (2) ◽  
pp. 476-479
Author(s):  
Donald C. Wigfield ◽  
Douglas M. Goltz
Keyword(s):  
Rate Constant ◽  
Copper Concentration ◽  
Copper Ions ◽  
Copper Ion ◽  
Order Rate Constant ◽  
First Order ◽  
Order Rate ◽  
Pseudo First Order ◽  
Rate Limiting ◽  
Kinetics Of

The kinetics of the reconstitution reaction of apotyrosinase with copper (II) ions are reported. The reaction is pseudo first order with respect to apoenzyme and the values of these pseudo first order rate constants are reported as a function of copper (II) concentration. Two copper ions bind to apoenzyme, and if the second one is rate limiting, the kinetically relevant copper concentration is the copper originally added minus the amount used in binding the first copper ion to enzyme. This modified copper concentration is linearly related to the magnitude of the pseudo first order rate constant, up to a copper concentration of 1.25 × 10−4 M (10-fold excess), giving a second order rate constant of 7.67 × 102 ± 0.93 × 102 M−1∙s−1.Key words: apotyrosinase, copper, tyrosinase.

The Role of Starting Potential in the Kinetics of Chemical Reactions under Electrodeless Discharge

1970 ◽  
Vol 25 (11) ◽  
pp. 1772
Author(s):  
T.S.R Ao ◽  
A. Patil
Keyword(s):  
Gas Phase ◽  
Chemical Reactions ◽  
Electric Discharge ◽  
Specific Rate ◽  
Gas Phase Reactions ◽  
Electrodeless Discharge ◽  
First Order ◽  
Kinetics Of

Abstract It has been shown that in kinetically first order gas phase reactions occuring under electric discharge, such as the decomposition of N2O, the application, at various initial pressures, of the same multiple of the respective starting potential ensures that the reaction occurs at the same specific rate.

scholarly journals Denaturation studies on natural and recombinant bovine prochymosin (prorennin)

1990 ◽  
Vol 271 (2) ◽  
pp. 541-547 ◽  
Author(s):  
R Sugrue ◽  
F A O Marston ◽  
P A Lowe ◽  
R B Freedman
Keyword(s):  
Inclusion Bodies ◽  
Kinetic Studies ◽  
Order Rate Constant ◽  
Slow Process ◽  
Equilibrium Studies ◽  
First Order ◽  
Denaturant Concentration ◽  
Recombinant Product ◽  
Stabilization Energies ◽  
Solubilization Of Inclusion Bodies

1. Prochymosin in solution in the presence of 8 M-urea is fully unfolded, as indicated by its fluorescence spectrum, fluorescence quenching behaviour and far-u.v.c.d. spectrum. 2. Equilibrium studies on the unfolding of prochymosin and pepsinogen by urea were carried out at pH 7.5 and pH 9.0. The results indicate that the stabilization energies of the two proteins are identical at pH 7.5, but that at pH 9.0 pepsinogen is significantly less stable than prochymosin. 3. Kinetic studies on the unfolding of prochymosin and pepsinogen indicate that the processes can be described by a single first-order rate constant, and that at any given value of denaturant concentration and pH the rate of unfolding of prochymosin is significantly greater than that of pepsinogen. 4. Unfolding of prochymosin by concentrated urea is not fully reversible, unlike that of pepsinogen. Kinetic analysis of the refolding of the proteins suggests the presence of a slow process following unfolding in urea; for pepsinogen this process leads to a slowly refolding form, whereas for prochymosin the slow process in urea leads to a form that cannot refold on dilution of the denaturant. 5. The results provide a rationale for an empirical process for recovery of recombinant prochymosin after solubilization of inclusion bodies in concentrated urea. 6. In all respects studied here, natural and recombinant bovine prochymosin were indistinguishable, indicating that the refolding protocol yields a recombinant product identical with natural prochymosin.

Kinetics of the Ozonation of Tetrabromobisphenol-A in Wastewater

2011 ◽  
Vol 383-390 ◽  
pp. 2945-2950 ◽  
Author(s):  
Jie Zhang ◽  
Shi Long He ◽  
Mei Feng Hou ◽  
Li Ping Wang ◽  
Li Jiang Tian
Keyword(s):  
Rate Constants ◽  
Apparent Rate Constant ◽  
Reaction Rate ◽  
Batch Reactor ◽  
Kinetic Studies ◽  
Tetrabromobisphenol A ◽  
First Order ◽  
Reaction Rate Constants ◽  
Pseudo First Order ◽  
Kinetics Of

The kinetics of TBBPA degradation by ozonation in semi-batch reactor was studied. The reaction rate constants of TBBPA with O3 and •OH were measured by means of direct ozone attack and competition kinetics, and the values of which were 6.10 l/(mol•s), 4.8×109 l/(mol•s), respectively. Results of kinetic studies showed that TBBPA degradation by ozonation under the different conditions tested followed the pseudo-first-order. The values of apparent rate constant of TBBPA degradation increased with the increase of ozone dosage and pH, but decreased with the increase of initial TBBPA concentration.

scholarly journals Purification and kinetic mechanism of the major glutathione S-transferase from bovine brain

1989 ◽  
Vol 257 (2) ◽  
pp. 541-548 ◽  
Author(s):  
P R Young ◽  
A V Briedis
Keyword(s):  
Decanoic Acid ◽  
Kinetic Mechanism ◽  
Order Rate Constant ◽  
Bovine Brain ◽  
Glutathione S Transferase ◽  
Rate Acceleration ◽  
Hydrophobic Binding ◽  
Kinetics Of ◽  
Kinetics Of Inhibition

The major glutathione S-transferase isoenzyme from bovine brain was isolated and purified approx. 500-fold. The enzyme has a pI of 7.39 +/- 0.02 and consists of two non-identical subunits having apparent Mr values of 22,000 and 24,000. The enzyme is uniformly distributed in brain, and kinetic data at pH 6.5 with 1-chloro-2,4-dinitrobenzene (CDNB) as substrate suggest a random rapid-equilibrium mechanism. The kinetics of inhibition by product, by GSH analogues and by NADH are consistent with the suggested mechanism and require inhibitor binding to several different enzyme forms. Long-chain fatty acids are excellent inhibitors of the enzyme, and values of 1nKi for hexanoic acid, octanoic acid, decanoic acid and lauric acid form a linear series when plotted as a function of alkyl chain length. A free-energy change of -1900 J/mol (-455 cal/mol) per CH2 unit is calculated for the contribution of hydrophobic binding energy to the inhibition constants. The turnover number of the purified enzyme dimer is approx. 3400/min. When compared with the second-order rate constant for the reaction between CDNB and GSH, the enzyme is providing a rate acceleration of about 1000-fold. The role of entropic contributions to this small rate acceleration is discussed.

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