Laccase-mediated hydrophilization of lignin decreases unproductive enzyme binding but limits subsequent enzymatic hydrolysis at high substrate concentrations

One of the predominant mechanisms by which lignin restricts effective enzymatic deconstruction of lignocellulosic materials is the unproductive adsorption of enzymes. Although this inhibition can be partially mitigated through hydrophilization of lignin during thermochemical pretreatment, these types of treatments could potentially worsen slurry rheology, consequently making it more difficult to process the material at high substrate concentrations. In the work reported here, laccases were used to specifically modify lignin hydrophilicity within steam-pretreated substrate via in situ phenolic compound grafting. While lignin hydrophilization reduced unproductive enzyme adsorption, high-solids hydrolysis efficiency decreased significantly due to mass transfer limitations. It was apparent that low-solids hydrolysis experiments were a poor predictor of substrate digestibility at high-solids conditions and that substrate-water interactions impacted both substrate digestibility and slurry rheology.