Sulfonated lignin could inhibit the catalytic efficiency of β-etherase LigF significantly, not for Cα-dehydrogenase LigD.
Sulfonated lignin samples with larger molecular weight had prior impact on the catalytic efficiency of β-etherase LigF.
Hydrophobic interactions and ionic bond interactions were responsible for the increased adsorption of the enzymes to sulfonated lignin.
Nonspecific adsorption between protein and sulfonated lignin with different molecular weights did exist.