The interactions of Trichoderma cellulase enzyme activities in biomass conversion

Three strains of Trichoderma (T. reesei, T. viride, and T. harzianum) were evaluated for cellulase enzyme production and activity. Different cellulose substrates, including Avicel, carboxymethyl cellulose (CMC), bacterial cellulose (BC), and Whatman No. ۱ filter paper, were used to assess cellulase activity. Structural characterization of the substrates was performed using FT-IR, XRD, and SEM analyses. Results showed that bacterial cellulose possessed finer fibers and lower crystallinity than Avicel, making it more accessible to enzymatic degradation. The highest activities of endoglucanase (CMCase), exoglucanase (Avicelase), and total cellulase (BCase and FPase) were observed in T. reesei, T. viride, and T. harzianum, respectively. SDS-PAGE analysis revealed the presence of key cellulolytic enzymes, including cellobiohydrolases (CBHs), endoglucanases (EGs), and β-glucosidases (BGLs). Significant synergistic effects among these enzymes were detected, particularly in T. harzianum, resulting in enhanced cellulase activity. The study demonstrated that bacterial cellulose is a superior substrate for total cellulase activity assays compared with Avicel and filter paper. Overall, cellulase efficiency was strongly influenced by substrate properties, enzyme composition, and synergistic interactions among cellulolytic enzymes.

کلیدواژه ها:

Cellulase ، FTIR ، XRD ، T. reesei ، T. viride ، T. harzianum