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Primarystudies on several cellulase components with special characteristics purified from Trichoderma pseudokoningii S38
Author(s) -
Dong Wang,
Yinbo Qu,
Peiji Gao
Publication year - 1997
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1997.tb00431.x
Subject(s) - cellobiose , cellulase , sephadex , hydrolysis , cellulose , chemistry , enzyme , chromatography , specific activity , trichoderma , substrate (aquarium) , biochemistry , botany , biology , ecology
Ten cellulase components, consisting of five different endoglucanases (EG1ŐEG5), three cellobiohydrolases (CBH1, CBHX‐1 and CBHX‐2) and two b‐glucosidases (bG1 and bG2) from Trichoderma pseudokoningii S38, were successively purified by Sephadex G‐50, DEAE‐Sephadex A25 and finally by DEAE‐HPLC‐8HR column chromatography. The purified enzyme components were characterized with repect to their molecular mass, pI and, especially, substrate specificities. EG1 and EG2 were the main endoglucanases and were similar to other EGs obtained previously. However, EG5 showed the highest activity for forming short fibres from absorbent cotton, although its ability to hydrolyse carboxymethylcellulose to produce reducing sugars was very poor. Two new CBHs, termed CBHX‐1 and CBHX‐2, had characteristics different from those of CBHI and CBHII. CBHX‐1 showed a lower ability to hydrolyse absorbent cotton to produce cellobiose than other CBHs, but it had strong synergistic action with CBHI for the hydrolysis of crystalline cellulose. Compared with bG1, bG2 had a higher transglycosidase activity and a lower ability to hydrolyse cellobiose to glucose. The specificities of these ten components for a range of substrates were determined.