Characteristics of free endoglucanase and glycosidases multienzyme complex from Fusarium verticillioides

•Fusarium verticillioides present at least one cellulase multienzyme complex.•Multienzyme complex contain two endoglucanases, one cellobiohydrolase and one xylanase.•Cellulase multienzyme complex and free endoglucanase are highly thermostable. A novel multienzyme complex, E1C, and a free endoglucanase, E2 (GH5), from Fusarium verticillioides were purified. The E1C contained two endoglucanases (GH6 and GH10), one cellobiohydrolase (GH7) and one xylanase (GH10). Maximum activity was observed at 80°C for both enzymes and they were thermostable at 50 and 60°C. The activation energies for E1C and E2 were 21.3 and 27.5kJ/mol, respectively. The KM for E1C was 10.25g/L while for E2 was 6.58g/L. Both E1C and E2 were activated by Mn2+ and CoCl2 while they were inhibited by SDS, CuSO4, FeCl3, AgNO4, ZnSO4 and HgCl2. E1C and E2 presented endo-β-1,3–1,4-glucanase activity. E1C presented crescent activity towards cellopentaose, cellotetraose and cellotriose. E2 hydrolyzed the substrates cellopentaose, cellotetraose and cellotriose with the same efficiency. E1C showed a higher stability and a better hydrolysis performance than E2, suggesting advantages resulting from the physical interaction between proteins.