Construction of a structural enzyme adsorption/kinetics model to elucidate additives associated lignin-cellulase interactions in complex bioconversion system.

Enzymatic hydrolysis is a rate-limiting process in lignocellulose biorefinery. The reaction involves complex enzyme-substrate and enzyme-lignin interactions in both liquid and solid phases, and has not been well characterized numerically. In this study, a kinetic model was developed to incorporate dynamic enzyme adsorption and product inhibition parameters into hydrolysis simulation. The enzyme adsorption coefficients obtained from Langmuir isotherm were fed dynamically into first-order kinetics for simulating the equilibrium enzyme adsorption in hydrolysis. A fractal and product inhibition kinetics was introduced and successfully applied to improve the simulation accuracy on adsorbed enzyme and glucose concentrations at different enzyme loadings, lignin contents, and in the presence of bovine serum albumin (BSA) and lysozyme. The model provided numerical proof quantifying the beneficial effects of both additives, which improved the hydrolysis rate by reducing the nonproductive adsorption of enzyme on lignin. The hydrolysis rate coefficient and fractal exponent both increased with increasing enzyme loadings, and lignin inhibition exhibited with increasing fractal exponent. Compared with BSA, the addition of lysozyme exhibited higher hydrolysis rates, which was reflected in the larger hydrolysis rate coefficients and smaller fractal exponents in the simulation. The model provides new insights to support process development, control, and optimization.