Production of manganese peroxidase and laccase in a solid-state bioreactor and modeling of enzyme production kinetics

Abstract

Lignin-modifying enzymes have various promising applications such as biobleaching, biopulping, the functionalization of lignocellulosic materials, the modification of wood fibers, the remediation of contaminated soil and effluents, as well as improvement of the enzymatic hydrolysis of lignocellulosic substrates. In this study, the production of laccase and manganese peroxidase (MnP) in solid-state cultivation was examined. Oat husks were used as an inexpensive substrate for the white-rot fungus Cerrena unicolor PM170798 (FBCC 387). The addition of a fines fraction (consisting of oat flour and finely ground husks) enhanced MnP production fivefold and laccase production almost threefold. The enzyme production was studied first on a 100g scale, and the cultivation experiments were then repeated at a larger laboratory-scale (4kg) in a solid-state bioreactor. High enzyme activity levels were obtained (MnP: 340nkatg(-1)DM, laccase: 470nkatg(-1)DM). In addition, the correlation between the CO2 evolution rate and enzyme production was mathematically modeled from the bioreactor experimental data. The model parameters could be used to predict enzyme production.