Two moments preserving sectional approach for an enzymatic coagulation equation

The coagulation process has found extensive applications in monitoring the evolution of aerosol and granule preparation in pharmaceutical sciences, blood clotting in biology, and cheese manufacturing due to the enzymes in the dairy industry. Among these, modeling the cheese manufacturing process is more challenging due to three indistinguishable sub-mechanisms: (a) enzymatic proteolysis, (b) coagulation, and (c) gelation, which occurs during the enzymatic coagulation of milk. The current study focuses on developing a sectional approach based on the cell average technique for monitoring the evolution of enzyme-induced coagulation of paracasein micelles over time. The proposed technique preserves two integral properties, such as total number and total volume in the system. The mathematical formulation of the proposed technique is very simple, easy to code, and has a robust implementation on any uniform and non-uniform grids. Due to the unavailability of the analytical solutions of the number density functions, the validation of the new proposed approach is done by extracting the new series solutions through the modification of the Homotopy perturbation method [Kaur et al., J. Phys. A 52(38), 385201 (2019)] and exact integral moments for several kernels. It has been shown that the new approach not only estimates the first two integral moments accurately but also computes the second-order moment with high precision without any specific measures. Moreover, domains of varying size grids are taken into account to analyze the convergence behavior of the average-size paracasein micelles formed in the system based on the zeroth and first moments.