Theoretical analysis of intrinsic reaction kinetics and the behavior of immobilized enzymes system for steady-state conditions

Praveen, T.; Valencia, Pedro; Rajendran, L.

doi:10.1016/j.bej.2014.08.001

Cited by 23 publications

(21 citation statements)

References 20 publications

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“…Formulation/development of the mathematical models with assumptions like temperature, enzyme distribution, quantity, diffusivity, catalytic particle type, etc., have extensively discussed by D.Jeison et.al, [21]. To the progress, analytical solution to mathematical models that representing different mechanisms have been derived using MADM by T.Praveen et.al, [22]. Now, we take up the dimensionless form of mass balance equations for each kinetic model which is provided in [22].…”

Section: Solutions To the Reaction Kinetic Models By Agmmentioning

confidence: 99%

“…Praveen et al [22] reported that these mathematical models had been solved implementing MADM and discussed the validation of the solution in addition to the translation of error to mean integrated effectiveness factor. In the current study, a comparison is made between the solutions obtained by MADM [22] and AGM. Additionally, it is compared to a MATLAB-based numerical simulation program.…”

Section: Introductionmentioning

confidence: 99%

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A study on various types of immobilization of enzyme kinetic mechanisms by comparing with the solutions obtained from AGM and MADM

Saravanakumar,

Veeramuni,

Veeramani

et al. 2024

Preprint

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In this article, the kinetic mechanisms are based on Michaelis-Menten reaction in presence of substrate inhibition have been solved by techniques ‘Akbari-Ganji’s Method’ (AGM) and ‘Modified Adomian decomposition method’ (MADM). Comparisons of solution of dimensionless substrate and product concentrations for various kinetic mechanisms have been carried out using AGM, MADM and numerical simulation. We assessed the impact of Thiele modulus, dimensionless inhibition degree, and concentration of substances outside the support on changing nature of substrate and product concentrations within the boundary layer in this study. The obtained results depict that the used methods have good accuracy for different values of kinetic parameters. Furthermore, the mean integrated effectiveness factor has been derived for all the mechanisms employing AGM solutions. This paper clearly illustrates the distinctions between MADM and AGM.

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Section: Solutions To the Reaction Kinetic Models By Agmmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A study on various types of immobilization of enzyme kinetic mechanisms by comparing with the solutions obtained from AGM and MADM

Saravanakumar,

Veeramuni,

Veeramani

et al. 2024

Preprint

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“…Heterogeneous catalysis using immobilized penicillin acylase in porous supports is modeled using the mass conservation equation inside catalyst particles. The resulting reaction-diffusion equations for the substrate and for both products, considering spherical particles, are shown in Equations (23)- (25):…”

Section: Theorymentioning

confidence: 99%

“…Modified Adomian decomposition method [24,25]: The method has been widely used as a solution method for nonlinear differential problems, where it cannot always satisfy the boundary conditions imposed (applicability limitations) and also has the added complexity of calculation of the Adomian polynomials, which are usually impractical to apply.…”

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confidence: 99%

Estimation of the Effectiveness Factor for Immobilized Enzyme Catalysts through a Simple Conversion Assay

Valencia

Ibáñez

2019

Catalysts

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A novel methodology to estimate the effectiveness factor (EF) of an immobilized enzyme catalyst is proposed here. The methodology consists of the determination of the productivity of both the immobilized enzyme catalyst and its corresponding soluble enzyme, plotted as a function of the reaction conversion. The ratio of these productivities corresponds to the EF estimator of the catalyst. Conversion curves were simulated in a batch reactor with immobilized enzyme and soluble enzyme for different values of the S0/KM ratio and Thiele modulus (Φ) to demonstrate this hypothesis. Two different reaction orders were tested: first-order kinetic and Michaelis–Menten-based kinetic with product inhibition. The results showed that the ratio of productivities between the immobilized and soluble enzymes followed the behavior profile presented by the EF with satisfactory agreement. This simple methodology to estimate the EF is based on routine conversion experiments, thus avoiding the exhaustive kinetic and mass transfer characterization of the immobilized enzyme catalyst.

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“…The only difference between these two models is that in the Russo et al model has a denominator term which subtract the substrate concentration in equilibrium with the product concentration ‫ܥ‬ ௌ . Russo et al [12] took this expression from the work of Praveen et al [13] where it is regarded as reversible Michaelis Menten kinetic. In the work of Segel [14], the kinetic expression derived for a reversible reaction is the same form as derived in this work and described in in Eq.…”

Section: 2reversible Michaelis Menten Kineticsmentioning

confidence: 99%

CO2 mass transfer model for carbonic anhydrase-enhanced aqueous MDEA solutions

Gladis

Gundersen

Neerup

et al. 2018

Chemical Engineering Journal

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Theoretical analysis of intrinsic reaction kinetics and the behavior of immobilized enzymes system for steady-state conditions

Cited by 23 publications

References 20 publications

A study on various types of immobilization of enzyme kinetic mechanisms by comparing with the solutions obtained from AGM and MADM

A study on various types of immobilization of enzyme kinetic mechanisms by comparing with the solutions obtained from AGM and MADM

Estimation of the Effectiveness Factor for Immobilized Enzyme Catalysts through a Simple Conversion Assay

CO2 mass transfer model for carbonic anhydrase-enhanced aqueous MDEA solutions

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