The overall objective of this research is to identify and optimize enzymatic applications that have the potential to degrade middle lamella lignin, so as to decrease economic and environmental costs associated with the production of mechanical pulp. Non-productive binding of enzyme to lignin in lignocellulosic biomass reduces enzyme availability and efficiency. The elucidation of non-productive binding behavior between hydrolytic enzymes and lignocellulosic substrates could significantly improve the efficiency of corresponding industrial bioprocesses. The first part of this report presents a study that characterizes non-catalytic interactions between enzymes and fibre. The second part of this report presents the biochemical and mutational studies of a novel, small laccase SCO6712 from Streptomyces coelicolor. The findings from this research support the design, control, and optimization of enzymatic treatments of lignocellulosic fibres in the pulp and biofuel industries.

The overall objective of this research is to identify and optimize enzymatic applications that have the potential to degrade middle lamella lignin, so as to decrease economic and environmental costs associated with the production of mechanical pulp. Non-productive binding of enzyme to lignin in lignocellulosic biomass reduces enzyme availability and efficiency. The elucidation of non-productive binding behavior between hydrolytic enzymes and lignocellulosic substrates could significantly improve the efficiency of corresponding industrial bioprocesses. The first part of this report presents a study that characterizes non-catalytic interactions between enzymes and fibre. The second part of this report presents the biochemical and mutational studies of a novel, small laccase SCO6712 from Streptomyces coelicolor. The findings from this research support the design, control, and optimization of enzymatic treatments of lignocellulosic fibres in the pulp and biofuel industries.