Isothermal reaction calorimetry as a tool for kinetic analysis

2004 ◽  
Vol 419 (1-2) ◽  
pp. 1-17 ◽  
Author(s):  
Andreas Zogg ◽  
Francis Stoessel ◽  
Ulrich Fischer ◽  
Konrad Hungerbühler
RSC Advances ◽  
2018 ◽  
Vol 8 (6) ◽  
pp. 3286-3295 ◽  
Author(s):  
A. S. Portnyagin ◽  
A. P. Golikov ◽  
V. A. Drozd ◽  
V. A. Avramenko

Presented method of kinetic analysis of non-isothermal reaction data provides precise kinetic parameters for different materials with different morphology and particle size.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Juan P. Yasnó ◽  
Susana Conconi ◽  
Arnaldo Visintin ◽  
Gustavo Suárez

AbstractNon-isothermal reaction mechanism and kinetic analysis for the synthesis of monoclinic lithium zirconate (m-Li2ZrO3) were investigated by processing of TG-DTA, along with XRD, DLS, and HRTEM. For this purpose, the solid-state reaction of Li2CO3 with ZrO2 was carried out by TG-DTA at different heating rates (10, 20, and 30 °C/min) from room temperature to 1100 °C. The thermal data was used to calculate the kinetic parameters by two types of isoconversional methods: Flynn-Wall-Ozawa (FWO) and Kissinger-Akahira-Sunose (KAS). The reaction mechanism was determined by the model-fitting method, applying the Coats-Redfern (CR) approximation to the different solid-state reaction models. The results confirmed the formation of pure m-Li2ZrO3, consists of semispherical particles of about 490 nm, using a very short reaction time. The average activation energy obtained by FWO and KAS methods were 274.73 and 272.50 kJ/mol, respectively. It was found that the formation of m-Li2ZrO3 from Li2CO3 with ZrO2 is governed by the three-dimensional diffusion mechanism. Based on these results, a microscopic reaction model of the formation of m-Li2ZrO3 was proposed.


1965 ◽  
Vol 13 (01) ◽  
pp. 155-175 ◽  
Author(s):  
H. C Hemker ◽  
P.W Hemker ◽  
E. A Loeliger

SummaryApplication of the methods of enzyme-kinetic analysis to the results of clotting tests is feasible and can yield useful results. However, the standard methods of enzyme kinetics are not applicable without modifications imposed by the peculiarities of the blood-clotting enzyme system. The influence of the following complicating circumstances is calculated :1. Substrate is not present in excess.2. Only relative measures exist for concentrations of substrate or enzymes.3. Enzymes and substrates are often added together.4. Reagents are not pure.5. Clotting-time is our only measure for clotting-velocity.Formulas are deduced, which makes it possible to recognize the effect of these complications.


1995 ◽  
Vol 32 (4) ◽  
pp. 225-231 ◽  
Author(s):  
Toru HARIGAI ◽  
Shinya KIMURA ◽  
Shuichi KAKURAI
Keyword(s):  

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