Cellulase secretion from a hyper-cellulolytic mutant of Trichoderma reesei Rut-C30 |
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Authors: | Ghosh Arati Ghosh B K Trimino-Vazquez H Eveleigh D E Montenecourt Bland S |
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Institution: | (1) Department of Physiology and Biophysics, UMDNJ-Rutgers Medical School, P.O. Box 101, 08854 Piscataway, NJ, USA;(2) Department of Biochemistry and Microbiology, Cook College, Rutgers-The State University, 08903 New Brunswick, NJ, USA;(3) Department of Biology and Biotechnology Research Center, Lehigh University, 18015 Bethlehem, PA, USA |
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Abstract: | Two strains of Trichoderma reesei, wild type QM6a and mutant Rut-C30, were grown in meida containing an inducer, insoluble crystalline cellulose (Avicel PH101), as carbon source for 11 days. The cell growth, expressed as myceliar protein content, of Rut-C30 was 4–5 times higher than QM6a. The lack of ultrastructural disorganization, and absence of intracellular enzyme release into the growth medium, indicated that none of these two strains had undergone any significant autolysis during the entire growth phase. Cellulase activities, mainly endoglucanase, cellobiase and filter paper degrading activity (disc) were enhanced in Rut-C30 cells. A major change was observed in the endoglucanase activity which was 30 times higher in Rut-C30 than QM6a, whereas, both -glucosidase and disc activities were 3 times enhanced in Rut-C30 compared to QM6a. In addition to synthesis, cellulase secretion was also enhanced in Rut-C30. Both the organisms contained same amounts of intracellular marker enzyme activities (e.g., inosine diphosphatase, thiamine pyrophosphatase, alkaline phosphatase). Finally, the enahncement of secretory activity of Rut-C30 was correlated with the proliferation of rough endoplasmic reticulum (RER) and increased phospholipid content. It appears that Rut-C30 is not only a hypercellulolytic but also a hypersecretor mutant. |
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Keywords: | Cellulase secretion |
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