Irreversible thermoinactivation of cellobiohydrolase I from Trichoderma reesei has been analyzed at 70Β°C and pH 4.8. The time course of thermal inactivation and the dependence of the inactivation rates on protein concentration suggested that aggregation followed by precipitation was the main process
Pectinase from Trichoderma reesei QM 9414
β Scribed by T. Haltmeier; M. Leisola; D. Ulmer; R. Waldner; A. Fiechter
- Publisher
- John Wiley and Sons
- Year
- 1983
- Tongue
- English
- Weight
- 279 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0006-3592
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The microscopic morphology of Trichoderma reesei OM 9414, growing in submerged culture, was studied by image analysis. The morphology was characterized by the total hyphal length, the total number of tips, the number of actively growing tips, and the length of the main hypha. To describe the growth
The separation and purification method of extracellular cellobiase and aryl-8-glucosidase from Trichoderma reesei by means of affinity chromatography on controlled porosity glass activated by 7aminopropyltriethoxysilane and oxiranes are described.
The action of cellobiohydrolase I [(1+4)-/I-n-glucan cellobiohydrolase, EC 3.2.1.91, CBH-I] from Trichoderma reesei QM 9414 on cello-oligosaccharides labelled with tritium in the reducing moiety has been investigated. There was a marked preference of CBH-I to attack the first three linkages at the r