文献类型：期刊文献

英文题名：Identification and purification of the main components of cellulases from a mutant strain of Trichoderma viride T 100-14

作者：Zhou, Jin[1];Wang, Yong-Hong[1];Chu, Ju[1];Zhuang, Ying-Ping[1];Zhang, Si-Liang[1];Yin, Peng[1]

机构：[1]E China Univ Sci & Technol, Natl Res Ctr Biotechnol Shanghai, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2008

卷号：99

期号：15

起止页码：6826

外文期刊名：BIORESOURCE TECHNOLOGY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000257367600013)】；

语种：英文

外文关键词：Trichoderma viride T 100-14; mutant strain; cellulase; identification; purification

摘要：A new mutant strain of fungus Trichoderma viride T 100-14 was cultivated on 1% microcrystalline cellulose (Avicel) for 120 It and the resulting culture filtrate was prepared for protein identification and purification. To identify the predominant catalytic components, cellulases were separated by an adapted two-dimensional electrophoresis technique. The apparent major spots were identified by high performance liquid chromatography electrospray ionization mass (HPLC-ESI-MS). Seven of the components were previously known, i.e., the endoglucanases Ce17B (EG I), Cel12A (EG III), Cel61A (EG IV), the cellobiohydrolases Cel7A (CBH I), Cel6A (CBH II), Cel6B (CBH IIb) and the beta-glucosidase. The seven major components in the fermentation broth of T viride T 100-14 probably constitute the essential enzymes for crystalline cellulose hydrolysis and they were further purified to electrophoretic homogeneity by a series of chromatography column. Hydrolysis studies of the purified elements revealed that three of the cellulases were classified as cellobiohydrolases due to their main activities on p-nitrophenyl-beta-D-cellobioside (pNPC). Three of the cellulases, with the abilities of hydrolyzing both carboxymethyl-cellulose (CMC) and Avicel indicate their endoglucanase activities. It deserved noting that the beta-glucosidase from the T 100-14 displayed an extremely high activity on p-nitrophenyl-beta-D-glycopyranoside (pNPG), which suggested it was a good candidate for the conversion of cellobiose to glucose. (C) 2008 Elsevier Ltd. All rights reserved.