Abstract
Lignin is Nature’s major source of aromatic chemistry and is by many seen as the green entry-point alternative to the fossil-based chemical industry. Due to its chemically recalcitrant structure, the utilization of lignin is challenging, wherein enzymes might be the key to overcome this challenge. Here, we focus on the characterization of dye-decolorizing peroxidases from Streptomyces coelicolor A3(2) (ScDyPs) in the context of enzymatic modification of organosolv lignins from aspen and Miscanthus × giganteus. In this study, we show that the ScDyPB can remodel organosolv lignins from grassy biomass, leading to higher molecular weight species, while ScDyPAs can deconstruct hardwood lignin, leading to an overall reduction in its molecular weight. Additionally, we show that ScDyPB is effective in polymerizing low-molecular-weight phenolics, leading to their removal from the solution.