Inhibition of enzymatic hydrolysis by residual lignins from softwood—study of enzyme binding and inactivation on lignin‐rich surface

• DOI: 10.1002/bit.23242
• Publication Date: 2011-06-23T12:41:59Z
• Authors: Jenni Rahikainen; Saara Mikander; Kaisa Marjamaa; Tarja Tamminen; Angelos Lappas; Liisa Viikari; Kristiina Kruus
• Keywords: Softwood; Enzymatic Hydrolysis; Hemicellulose

Lignin-derived inhibition is a major obstacle restricting the enzymatic hydrolysis of cell wall polysaccharides especially with softwood lignocellulosics. Enzyme adsorption on lignin suggested to contribute inhibitory effect lignin. The interaction cellulases was studied in present work commercial Trichoderma reesei (Celluclast) and lignin-rich residues isolated from steam pretreated (SPS) by acid hydrolysis. Both preparations inhibited microcrystalline cellulose (Avicel) adsorbed cellulase mixture. phenomenon at low temperature (4°C) typical (45°C) following activities free lignin-bound enzymes. Severe inactivation enzymes observed 45°C, however 4°C retained well their activity. Furthermore, SDS-PAGE analysis indicated that very strong interactions form between residue because were not released electrophoresis. These results suggest heat-induced denaturation may take place surface temperature.