Beyond conventional models: integer and fractional order analysis of nonlinear Michaelis-Menten kinetics in immobilised enzyme reactors

Abstract

Purpose

This study explores the immobilisation of enzymes within porous catalysts of various geometries, including spheres, cylinders and flat pellets. The objective is to understand the irreversible Michaelis-Menten kinetic process within immobilised enzymes through advanced mathematical modelling.

Design/methodology/approach

Mathematical models were developed based on reaction-diffusion equations incorporating nonlinear variables associated with Michaelis-Menten kinetics. This research introduces fractional derivatives to investigate enzyme reaction kinetics, addressing a significant gap in the existing literature. A novel approximation method, based on the independent polynomials of the complete bipartite graph, is employed to explore solutions for substrate concentration and effectiveness factor across a spectrum of parameter values. The analytical solutions generated through the bipartite polynomial approximation method (BPAM) are rigorously tested against established methods, including the Bernoulli wavelet method (BWM), Taylor series method (TSM), Adomian decomposition method (ADM) and fourth-order Runge-Kutta method (RKM).

Findings

The study identifies two main findings. Firstly, the behaviour of dimensionless substrate concentration with distance is analysed for planar, cylindrical and spherical catalysts using both integer and fractional order Michaelis-Menten modelling. Secondly, the research investigates the variability of the dimensionless effectiveness factor with the Thiele modulus.

Research limitations/implications

The study primarily focuses on mathematical modelling and theoretical analysis, with limited experimental validation. Future research should involve more extensive experimental verification to corroborate the findings. Additionally, the study assumes ideal conditions and uniform catalyst properties, which may not fully reflect real-world complexities. Incorporating factors such as mass transfer limitations, non-uniform catalyst structures and enzyme deactivation kinetics could enhance the model’s accuracy and broaden its applicability. Furthermore, extending the analysis to include multi-enzyme systems and complex reaction networks would provide a more comprehensive understanding of biocatalytic processes.

Practical implications

The validated bipartite polynomial approximation method presents a practical tool for optimizing enzyme reactor design and operation in industrial settings. By accurately predicting substrate concentration and effectiveness factor, this approach enables efficient utilization of immobilised enzymes within porous catalysts. Implementation of these findings can lead to enhanced process efficiency, reduced operating costs and improved product yields in various biocatalytic applications such as pharmaceuticals, food processing and biofuel production. Additionally, this research fosters innovation in enzyme immobilisation techniques, offering practical insights for engineers and researchers striving to develop sustainable and economically viable bioprocesses.

Social implications

The advancement of enzyme immobilisation techniques holds promise for addressing societal challenges such as sustainable production, environmental protection and healthcare. By enabling more efficient biocatalytic processes, this research contributes to reducing industrial waste, minimizing energy consumption and enhancing access to pharmaceuticals and bio-based products. Moreover, the development of eco-friendly manufacturing practices through biocatalysis aligns with global efforts towards sustainability and mitigating climate change. The widespread adoption of these technologies can foster a more environmentally conscious society while stimulating economic growth and innovation in biotechnology and related industries.

Originality/value

This study offers a pioneering approximation method using the independent polynomials of the complete bipartite graph to investigate enzyme reaction kinetics. The comprehensive validation of this method through comparison with established solution techniques ensures its reliability and accuracy. The findings hold promise for advancing the field of biocatalysts and provide valuable insights for designing efficient enzyme reactors.