The adsorption properties of endoglucanase to lignin and their impact on hydrolysis

Nonproductive adsorption of cellulase to lignin dramatically influenced the hydrolysis efficiency of lignocellulose. By comparing the adsorption behaviors of CBH and EG, we found that the adsorption of EG to lignin showed lower adsorption velocity and capacity versus CBH. During the adsorption of EG to lignin, carbohydrate binding domain (CBM) and catalytic domain (CD) both played an important role by a two-step adsorption process, in which CD slowly bond on lignin and developed stronger interaction with lignin. The optimal binding position of EG on lignin was consistent with that on polysaccharide located in the open catalytic tunnel. So, the adsorption of EG to lignin not only limited the movement of enzyme, but also restricted the catalytic ability of enzyme, which dramatically influenced enzymatic hydrolysis. Increasing the proportion of EG in cellulase cocktails or engineering “weak lignin adsorbed” EG was necessary to relieve the influence of lignin adsorption on hydrolysis.