COMPARATIVE SECRETOME ANALYSIS OF TRICHODERMA REESEI QM9414 GROWN ON SEVERAL DIFFERENT CARBON SOURCES
The filamentous fungus Trichoderma reesei is widely used in industrial source of proteins and plays an important role because of its ability to secrete large amounts of cellulases and hemicellulases. To provide an overview of secreted protein information by T. reesei, profiles of extracellular proteins at 1％ Kraft pulp from 0 to 120 h incubation were analyzed by two-dimensional gel electrophoresis. A total of 11 protein spots at 120h were identified by peptide mass fingerprinting using matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. Among them were seven cellulases, an acetyl xylan esterase, an α-L-galactosidase, a chitinase and a β-xylosidase. Of them, CBHII presented at least three electrophoretic forms in 2D map. Differential displays of these proteins showed that their formations need different induction times. BXL was the earliest detected protein, followed by CBHI and EGI, CBHII and EGII. Moreover, we also reported a comprehensive secretome analysis in the presence of different carbon sources. The comparative analysis of secreted proteomes confirmed that the secretion of cellulases and hemicellulases was regulated by two ways: one is a low constitutive cellulase expression (CBHII) at all the carbon sources studied; the other is mass secretion of cellulases only induced by cellulose.
Trichoderma reesei cellulase secretome carbon sources protein spots
Ouyang Jia Liu Changqin Yan Ming Dong Zhenwei Xu Lin
College of Chemical Engineering, Nanjing Forestry University, Nanjing, 210009, China College of Life Science and Pharmacutical Engineering, Nanjing University of Technology,Nanjing, 210
国际会议
广州
英文
491-494
2010-11-08（万方平台首次上网日期，不代表论文的发表时间）