scholarly journals Waste-Derived Green Nanocatalyst for Biodiesel Production: Kinetic-Mechanism Deduction and Optimization Studies

2021 ◽  
Vol 13 (11) ◽  
pp. 5849
Author(s):  
Chee Yoong Chooi ◽  
Jia Huey Sim ◽  
Shiau Foon Tee ◽  
Zhi Hua Lee
Keyword(s):  
Active Sites ◽  
Reaction Rate ◽  
Surface Reaction ◽  
Pore Diameter ◽  
Preparation Method ◽  
Kinetic Mechanism ◽  
Transesterification Reaction ◽  
Biodiesel Production ◽  
Rate Limiting Step ◽  
Rate Limiting

This research focuses on deducing the kinetic mechanism for biodiesel production catalyzed by a CaO nanocatalyst derived from waste cockle shells via thermal hydration–dehydration treatment. In addition, the CaO nanocatalyst preparation method via thermal hydration–dehydration-related parameters (hydration duration, recalcination temperature, and recalcination duration) was studied and optimized. The transesterification reaction catalyzed by the CaO nanocatalyst followed the Langmuir–Hinshelwood kinetic mechanism with surface reaction as the rate-limiting step. The relatively low activation energy (3786.7 J/mol) for a transesterification reaction offered by the CaO nanocatalyst enhanced the reaction rate to 27.3% FAME yield/hr. The optimal conditions for the thermal hydration–dehydration treatment used to develop the nano CaO catalyst were 6 h of hydration duration, 650 °C of recalcination temperature, and 3 h of recalcination duration. Of biodiesel yield, 94.13% was obtained at a moderate temperature of 60 °C and 3 h reaction time during the transesterification of palm oil catalyzed by the nano-CaO. SEM, BET, and TPD results proved that the CaO nanocatalyst had a large surface area (13.9113 m2/g) and high pore volume (0.0318 cm3/g) that were rich in active sites (1046.46 μmol CO2/g), and the pore diameter (33.17 nm) was accessible to reactants and products.

scholarly journals Effect of the Preparation Method of LaSrCoFeOx Perovskites on the Activity of N2O Decomposition

2021 ◽  
Author(s):  
Nia Richards ◽  
Luke A. Parker ◽  
James H. Carter ◽  
Samuel Pattisson ◽  
David J. Morgan ◽  
...  
Keyword(s):  
Citric Acid ◽  
Active Sites ◽  
Preparation Method ◽  
N2o Decomposition ◽  
Oxygen Species ◽  
Calcination Temperatures ◽  
Highly Active ◽  
Rate Limiting Step ◽  
Enhanced Mobility ◽  
Rate Limiting

AbstractN2O remains a major greenhouse gas and contributor to global warming, therefore developing a catalyst that can decompose N2O at low temperatures is of global importance. We have investigated the use of LaSrCoFeOx perovskites for N2O decomposition and the effect of surface area, A and B site elements, Co–O bond strength, redox capabilities and oxygen mobility have been studied. It was found that by using a citric acid preparation method, perovskites with strong redox capabilities and weak Co–O bonds can be formed at relatively low calcination temperatures (550 °C) resulting in highly active catalysts. The enhanced activity is related to the presence of highly mobile oxygen species. Oxygen recombination on the catalyst surface is understood to be a prominent rate limiting step for N2O decomposition. Here the reduced strength of Co–O bonds and mobile lattice oxygen species suggest that the surface oxygen species have enhanced mobility, aiding recombination, and subsequent regeneration of the active sites. La0.75Sr0.25Co0.81Fe0.19Ox prepared by citric acid method converted 50% of the N2O in the feed (T50) at 448 °C. Graphic Abstract

scholarly journals Substrate specificity of sheep liver sorbitol dehydrogenase

1998 ◽  
Vol 330 (1) ◽  
pp. 479-487 ◽  
Author(s):  
I. Rune LINDSTAD ◽  
Peter KÖLL ◽  
John S. McKINLEY-McKEE
Keyword(s):  
Substrate Specificity ◽  
Ternary Complex ◽  
Kinetic Mechanism ◽  
Sorbitol Dehydrogenase ◽  
Hydroxyl Group ◽  
Enzyme Active Site ◽  
Sheep Liver ◽  
Rate Limiting Step ◽  
Steady State Kinetics ◽  
Rate Limiting

The substrate specificity of sheep liver sorbitol dehydrogenase has been studied by steady-state kinetics over the range pH 7-10. Sorbitol dehydrogenase stereo-selectively catalyses the reversible NAD-linked oxidation of various polyols and other secondary alcohols into their corresponding ketones. The kinetic constants are given for various novel polyol substrates, including L-glucitol, L-mannitol, L-altritol, D-altritol, D-iditol and eight heptitols, as well as for many aliphatic and aromatic alcohols. The maximum velocities (kcat) and the substrate specificity-constants (kcat/Km) are positively correlated with increasing pH. The enzyme-catalysed reactions occur by a compulsory ordered kinetic mechanism with the coenzyme as the first, or leading, substrate. With many substrates, the rate-limiting step for the overall reaction is the enzyme-NADH product dissociation. However, with several substrates there is a transition to a mechanism with partial rate-limitation at the ternary complex level, especially at low pH. The kinetic data enable the elucidation of new empirical rules for the substrate specificity of sorbitol dehydrogenase. The specificity-constants for polyol oxidation vary as a function of substrate configuration with D-xylo > d-ribo > L-xylo > d-lyxo ≈ l-arabino > D-arabino > l-lyxo. Catalytic activity with a polyol or an aromatic substrate and various 1-deoxy derivatives thereof varies with -CH2OH >-CH2NH2 >-CH2OCH3 ≈-CH3. The presence of a hydroxyl group at each of the remaining chiral centres of a polyol, apart from the reactive C2, is also nonessential for productive ternary complex formation and catalysis. A predominantly nonpolar enzymic epitope appears to constitute an important structural determinant for the substrate specificity of sorbitol dehydrogenase. The existence of two distinct substrate binding regions in the enzyme active site, along with that of the catalytic zinc, is suggested to account for the lack of stereospecificity at C2 in some polyols.

scholarly journals Kinetic modelling of hydrogen transfer deoxygenation of a prototypical fatty acid over a bimetallic Pd60Cu40 catalyst: an investigation of the surface reaction mechanism and rate limiting step

2020 ◽  
Vol 5 (9) ◽  
pp. 1682-1693
Author(s):  
Kin Wai Cheah ◽  
Suzana Yusup ◽  
Martin J. Taylor ◽  
Bing Shen How ◽  
Amin Osatiashtiani ◽  
...  
Keyword(s):  
Oleic Acid ◽  
Reaction Mechanism ◽  
Hydrogen Transfer ◽  
Surface Reaction ◽  
Kinetic Modelling ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Cu Catalyst ◽  
P Application ◽  
Rate Limiting

Application of tetralin as a source of hydrogen for catalytic conversion of oleic acid to diesel-like hydrocarbons using a bimetallic Pd–Cu catalyst.

scholarly journals Human glutamic-γ-semialdehyde dehydrogenase. Kinetic mechanism

1989 ◽  
Vol 261 (3) ◽  
pp. 935-943 ◽  
Author(s):  
C Forte-McRobbie ◽  
R Pietruszko
Keyword(s):  
Kinetic Mechanism ◽  
Product Inhibition ◽  
Maximal Velocity ◽  
Semialdehyde Dehydrogenase ◽  
Rate Limiting Step ◽  
Dead End ◽  
Inhibition Studies ◽  
Rate Limiting ◽  
Competitive Pattern ◽  
Pattern Versus

The kinetic mechanism of homogeneous human glutamic-gamma-semialdehyde dehydrogenase (EC 1.5.1.12) with glutamic gamma-semialdehyde as substrate was determined by initial-velocity, product-inhibition and dead-end-inhibition studies to be compulsory ordered with rapid interconversion of the ternary complexes (Theorell-Chance). Product-inhibition studies with NADH gave a competitive pattern versus varied NAD+ concentrations and a non-competitive pattern versus varied glutamic gamma-semialdehyde concentrations, whereas those with glutamate gave a competitive pattern versus varied glutamic gamma-semialdehyde concentrations and a non-competitive pattern versus varied NAD+ concentrations. The order of substrate binding and release was determined by dead-end-inhibition studies with ADP-ribose and L-proline as the inhibitors and shown to be: NAD+ binds to the enzyme first, followed by glutamic gamma-semialdehyde, with glutamic acid being released before NADH. The Kia and Kib values were 15 +/- 7 microM and 12.5 microM respectively, and the Ka and Kb values were 374 +/- 40 microM and 316 +/- 36 microM respectively; the maximal velocity V was 70 +/- 5 mumol of NADH/min per mg of enzyme. Both NADH and glutamate were product inhibitors, with Ki values of 63 microM and 15,200 microM respectively. NADH release from the enzyme may be the rate-limiting step for the overall reaction.

Kinetic mechanism of phosphorylase a, II. Isotope exchange studies at equilibrium

1970 ◽  
Vol 48 (7) ◽  
pp. 755-758 ◽  
Author(s):  
H. D. Engers ◽  
W. A. Bridger ◽  
N. B. Madsen
Keyword(s):  
Exchange Rates ◽  
Isotope Exchange ◽  
Initial Rate ◽  
Kinetic Mechanism ◽  
Rabbit Muscle ◽  
Glucose Inhibition ◽  
Rate Limiting Step ◽  
Equilibrium Exchange ◽  
Muscle Phosphorylase ◽  
Rate Limiting

In order to confirm the kinetic mechanism which was proposed for rabbit muscle phosphorylase a on the basis of initial rate studies and UDP-glucose inhibition experiments, isotope exchange studies at equilibrium were performed, both in the presence and absence of the modifier AMP.Both the 14C-glucose [Formula: see text] and the [Formula: see text]1-phosphate equilibrium exchange rates increased to a maximum as the concentrations of the varied substrates became saturating, either in the presence or absence of AMP. The plateaus observed in these experiments indicate the lack of inhibition of the exchange of one pair of substrates when the concentration of the other substrate pair was raised, and confirms the proposed random addition of substrates to the enzyme.The fact that similar exchange rates were observed for either reaction direction reinforced the concept that rapid equilibrium conditions apply to the phosphorylase a mechanism; i.e. the interconversion of the ternary complexes tends to be the rate-limiting step in the reaction sequence.Maximal velocities determined from initial rate data reported in the previous paper agreed with those calculated from isotope exchange rates.

scholarly journals Chemical clustering and visualization applied to macromolecular crystallography

2014 ◽  
Vol 70 (a1) ◽  
pp. C1145-C1145
Author(s):  
Andrew Bruno ◽  
Amanda Ruby ◽  
Joseph Luft ◽  
Thomas Grant ◽  
Jayaraman Seetharaman ◽  
...  
Keyword(s):  
Hierarchical Clustering ◽  
High Throughput ◽  
Active Sites ◽  
X Ray Crystallography ◽  
Rate Limiting Step ◽  
Potential Applications ◽  
Crystallization Conditions ◽  
Electron Density Map ◽  
Distance Coefficient ◽  
Rate Limiting

Many bioscience fields employ high-throughput methods to screen multiple biochemical conditions. The analysis of these becomes tedious without a degree of automation. Crystallization, a rate limiting step in biological X-ray crystallography, is one of these fields. Screening of multiple potential crystallization conditions (cocktails) is the most effective method of probing a proteins phase diagram and guiding crystallization but the interpretation of results can be consuming. To aid this empirical approach a cocktail distance coefficient was developed to quantitatively compare macromolecule crystallization conditions and outcome. These coefficients were evaluated against an existing similarity metric developed for crystallization, the C6 metric, using both virtual crystallization screens and by comparison of two related 1,536-cocktail high-throughput crystallization screens. Hierarchical clustering was employed to visualize one of these screens and the crystallization results from an exopolyphosphatase-related protein from Bacteroides fragilis, (BfR192) overlaid on this clustering. This demonstrated a strong correlation between certain chemically related clusters and crystal lead conditions. While this analysis was not used to guide the initial crystallization optimization, it led to the re-evaluation of unexplained peaks in the electron density map of the protein and the insertion and correct placement of a sodium, potassium and phosphate atoms in the structure. With these in place, the resulting structure of the putative active site demonstrated features consistent with active sites of other phosphatases which are involved in binding the phosphoryl moieties of nucleotide triphosphates. The new distance coefficient appears to be robust in this application and coupled with hierarchical clustering and the overlay of crystallization outcome reveals information of biological relevance. While tested with a single example the potential applications appear promising.

scholarly journals Kinetics study of hydrazodicarbonamide synthesis reaction

2013 ◽  
Vol 19 (2) ◽  
pp. 273-279 ◽  
Author(s):  
Gh. Bakeri ◽  
M. Rahimnejad
Keyword(s):  
Reaction Rate ◽  
Second Step ◽  
Kinetics Study ◽  
Synthesis Reaction ◽  
Formation Reaction ◽  
Reaction Rate Constants ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Rate Limiting ◽  
Kinetics Of

In this study, the kinetics of hydrazodicarbonamide (HDCA) synthesis reaction was investigated. Hydrazodicarbonamide is prepared by reaction of urea and hydrazine in acidic medium. Synthesis of HDCA from urea and hydrazine is a two steps reaction. In the first step, semicarbazide is synthesized from the reaction of one mole of urea and one mole of hydrazine and in the second step, semicarbazide reacts with urea to produce hydrazodicarbonamide. By controlling the temperature and pH in the reaction, hydrazine concentration and the amount of produced hydrazodicarbonamide were measured and using these data, reaction rate constants were calculated. Based on this study, it was found that the semicarbazide formation reaction from hydrazine is the rate limiting step. Rate of semicarbazide synthesis is -r1 = 0.1396 [NH2NH2]0.5810 and the rate of hydrazodicarbonamide synthesis is -r2 = 0.7715 [NH2NHCONH2]0.8430.

A Molecular Dynamics Study of Primary Production from Shale Organic Pores

SPE Journal ◽  
2020 ◽  
Vol 25 (05) ◽  
pp. 2521-2533 ◽  
Author(s):  
Felipe Perez ◽  
Deepak Devegowda
Keyword(s):  
Fluid Transport ◽  
Pore Diameter ◽  
Fluid Model ◽  
Fluid Composition ◽  
Hydrocarbon Production ◽  
Rate Limiting Step ◽  
Wet Gas ◽  
Rate Limiting ◽  
Organic Pores

Summary We created a model of mature kerogen saturated with a black oil. Our fluid model spans light, intermediate, and long alkane chains; and aromatics, asphaltenes, and resins. The maximum pore diameter of our kerogen model is 2.5 nm. The insertion of a microfracture in the system allows us to study fluid transport from kerogen to the microfracture, which is the rate-limiting step in hydrocarbon production from shales. Our results indicate that the composition of the produced fluids changes with time, transitioning from a dry/wet gas to a gas condensate, becoming heavier with time. However, at any given time, the produced fluid is significantly lighter than the in-situ fluid. The species with the greatest mobility is methane, which is expected because it is the lightest molecule in the fluid and its ability to migrate is greater than that of all other fluid molecules. A sensitivity analysis shows that the produced fluid composition strongly depends on the initial composition of the fluids in organic pores.

scholarly journals Kinetic studies of formate dehydrogenase

1970 ◽  
Vol 120 (4) ◽  
pp. 763-769 ◽  
Author(s):  
D. Peacock ◽  
D. Boulter
Keyword(s):  
Carbon Dioxide ◽  
Formate Dehydrogenase ◽  
Kinetic Studies ◽  
Kinetic Mechanism ◽  
Product Inhibition ◽  
Reverse Reaction ◽  
Enzyme Form ◽  
Rate Limiting Step ◽  
Measurable Rate ◽  
Rate Limiting

1. The kinetic mechanism of formate dehydrogenase is a sequential pathway. 2. The binding of the substrates proceeds in an obligatory order, NAD+ binding first, followed by formate. 3. It seems most likely that the interconversion of the central ternary complex is extremely rapid, and that the rate-limiting step is the formation or possible isomerization of the enzyme–coenzyme complexes. 4. The secondary plots of the inhibitions with HCO3− and NO3− are non-linear, which suggests that more than one molecule of each species is able to bind to the same enzyme form. 5. The rate of the reverse reaction with carbon dioxide at pH6.0 is 20 times that with bicarbonate at pH8.0, although no product inhibition could be detected with carbon dioxide. The low rate of the reverse reaction precluded any steady-state analysis as the enzyme concentrations needed to obtain a measurable rate are of the same order as the Km values for NAD+ and NADH.

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