MtLPMO9V协同纤维素酶高效水解木质纤维素

Lytic polysaccharide monooxygenases (LPMOs) play a crucial role in biomass conversion by disrupting cellulose crystallinity and enhancing cellulase-mediated hydrolysis. In this study, an AA9 family LPMO (MtLPMO9V) derived from Myceliophthora thermophila was extensively investigated. The synergistic effect of MtLPMO9V was evaluated by co-saccharifying microcrystalline cellulose (MCC) and phosphoric acid-swollen cellulose (PASC) with the endoglucanase DtCelA. To further explore its synergistic potential, MtLPMO9V was tested in combination with the commercial cellulase cocktail Ctec2, as well as with acid/ alkali-catalyzed atmospheric glycerol organic solvent (ac/al-AGO) pretreated bagasse, to assess its effect on enhancing cellulase hydrolysis. Additionally, the performance of MtLPMO9V was examined under elevated temperatures using a two-step approach. The results demonstrated that MtLPMO9V significantly enhanced the saccharification efficiency of DtCelA on both MCC and PASC substrates. Moreover, MtLPMO9V improved the hydrolytic efficiency of Ctec2 on low-solids substrates and exhibited an even stronger effect under high-solids conditions, significantly increasing the hydrolysis yield. This enhancement may be attributed to MtLPMO9V\'s ability to modify lignocellulosic structures, thereby alleviating cellulase inhibition at high substrate loadings. Furthermore, the thermostability of MtLPMO9V was explored using a two-step strategy, highlighting its potential for integration with thermostable cellulases to develop high-temperature enzyme formulations for industrial biomass saccharification.