PRIMARY STUDIES ON SEVERAL CELLULASE COMPONENTS WITH SPECIAL CHARACTERISTICS PURIFIED FROM TRICHODERMA-PSEUDOKONINGII-S38

Ten cellulase components, consisting of five different endoglucanases (EG1-EG5), three cellobiohydrolases (CBH1, CBHX-1 and CBHX-2) and two beta-glucosidases (beta G1 and beta G2) from Trichoderma pseudokoningi i S38, were successively purified by Sephadex G-50, DEAE-Sephadex A25 and finally by DEAE-HPLC-8HR column chromatography, The purified enzym e components were characterized with repect to their molecular mass, p I and, especially, substrate specificities, EG1 and EG2 were the main endoglucanases and were similar to other EGs obtained previously, Howe ver, EG5 showed the highest activity for forming short fibres from abs orbent cotton, although its ability to hydrolyse carboxymethylcellulos e to produce reducing sugars was very poor, Two new CBHs, termed CBHX- 1 and CBHX-2, had characteristics different from those of C8HI and CBH II, CBHX-I showed a lower ability to hydrolyse absorbent cotton to pro duce cellobiose than other CBHs, but it had strong synergistic action with CBHI for the hydrolysis of crystalline cellulose, Compared with b eta G1, beta G2 had a higher transglycosidase activity and a lower abi lity to hydrolyse cellobiose to glucose, The specificities of these te n components for a range of substrates were determined.