A novel multienzyme complex, El and a free endoglucanase, E2 (GH5), from Fusarium verticillioides were purified. The E1(C) contained two endoglucanases (GH6 and GH10), one cellobiohydrolase (GH7) and one xylanase (CH10). Maximum activity was observed at 80 degrees C for both enzymes and they were thermostable at 50 and 60 degrees C. The activation energies for E1(C) and E2 were 21.3 and 27.5 kJ/mol, respectively. The Km for E1(C) was 10.25 g/L while for E2 was 6.58 g/L. Both E1(C) and E2 were activated by Mn2+ and CoCl2 while they were inhibited by SDS, CuSO4, FeCl3, AgNO4, ZnSO4 and HgCl2. E1(C) and E2 presented endo-beta-1,3-1,4-glucanase activity. E1(C) presented crescent activity towards cellopentaose, cellotetraose and cellotriose. E2 hydrolyzed the substrates cellopentaose, cellotetraose and cellotriose with the same efficiency. E1(C) showed a higher stability and a better hydrolysis performance than E2, suggesting advantages resulting from the physical interaction between proteins. (C) 2013 Published by Elsevier Ltd.