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Butanol, at sub-growth-inhibitory levels, caused a ca. 20 to 30% increase in fluidity of lipid dispersions from Clostridium acetobutylicum. When grown in the presence of butanol or into stationary phase, C. acetobutylicum synthesized increased levels of saturated acyl chains at the expense of unsaturated chains.  相似文献   
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Summary The cellulases produced under pH controlled fermentation conditions with 5% Solka Floc and cornsteep liquor as substrates by Trichoderma reesei wild type QM6a and two mutants, Rut-C30 and RL-P37, have been separated by isoelectric focusing in polyacrylamide gels. The total complement of secreted proteins of the two mutants was distinct from the parent. However, the number and isoelectric points of the various enzymes in the cellulase complex were unchanged in the mutants. All secreted proteins stained with Schiff's reagent which indicated they were glycoproteins. One mutant, Rut-C30, exhibited a dramatic shift in the CBH I proteins during the course of the fermentation. RL-P37 showed a two-fold increase in the specific activity of both the total cellulase complex and endoglucanase. In addition a productivity on the order of 100 IU/l/h was achieved. Co-produced with the cellulases were at least two acid proteases with differential activity towards azocoll and azocasein.  相似文献   
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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.  相似文献   
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  总被引:2,自引:6,他引:2  
The development of an agar plate screening technique has allowed the isolation of a range of mutants of Trichoderma reesei capable of synthesizing cellulase under conditions of high catabolite repression. The properties of one of these mutants (NG-14) is described to illustrate the use of this technique. NG-14 produced five times the filter paper-degrading activity per ml of culture medium and twice the specific activity per mg of excreted protein in submerged culture when compared with the best existing mutant, QM9414. NG-14 also showed enhanced endo-beta-glucanase and beta-glucosidase production. Although these mutants were isolated as cellulase producers in the presence of 5% glycerol on agar plates, in similar liquid medium, NG-14 exhibits only partial derepression of the cellulase complex. Since the proportions of filter paper activity, endo-beta-glucanase, and cellobiase were not the same in mutants NG-14 and QM9414, and the yields of each enzyme under conditions repressive for cellulase synthesis were different, differential control of each enzyme of the cellulase complex is implied. These initial results suggest that the selective technique for isolating hyper-cellulase-producing mutants of Trichoderma will be of considerable use in the development of commercially useful cellulolytic strains.  相似文献   
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The effects of ethanol and phenylethanol on the growth of and glycoprotein secretion by Trichoderma reesei were studied. Low levels (1.5%, vol/vol) of ethanol perturbed the glycosylation process, as shown by alterations in the isoelectric profile of the secreted proteins and a reduction in the rate of incorporation of mannose into oligosaccharides. In addition to these effects on posttranslational modification, ethanol drastically lowered the protein secretion level of a hypersecretory strain.  相似文献   
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