Understanding the Inhibition Mechanism of Lignin Adsorption to Cellulase in Terms of Changes in Composition and Conformation of Free Enzymes

The adsorption of lignin to cellulase is the major obstacle in sugar-platform conversion lignocellulosic bioresources. In this study, behavior untreated and pretreated samples from corn stover was investigated, particular effects on composition spatial conformation free enzymes were explored. results showed that pretreatments decreased hydrophobic groups contents lignin, i.e., aromatic ring, ether carbonyl, as well content ionizable group, carboxyl, which reduced its hydrophobicity negative charge density, thus weakening ability cellulase. mainly adsorbed CBHII component inhibit synergistic effect enzymes. Lignin altered position tryptophan residues enzymes, exposing them protein surface. addition, secondary structure altered, with a decrease alpha-helix an increase random coil content, loosening change degree correlated capacity low caused least damage enzyme, NaOH being best. It appears appropriate pretreatment chemical modification resist promising long-term pathway overcome inhibition during