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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 744 (1983), S. 135-140 
    ISSN: 0167-4838
    Keywords: (Trichoderma reesei) ; Cellulase ; Cellulose ; Endo-1,4-β-d-d-glucanase ; Extracellular enzyme ; Heterogeneity ; β-Glucosidase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 20 (1983), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The enrichment technique for the preparation of catabolite repression-resistant producers of cellulase from Trichoderma reesei is based on the submerged cultivation of mutagenized conidia on 2% (w/v) cellobiose or carboxymethyl-cellulose and in the presence of 0.5% (w/v) 2-deoxyglucose as the catabolite repressor. Conidia that are resistant towards the catabolite repressor can produce enzymes necessary for hydrolysis of used substrates and grow under the given conditions. They can be separated from the ungerminated conidia by filtration and used for the production of new conidia which are already enriched with catabolite repression-resistant mutants.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 27 (1985), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Exopolygalacturonase, endopolygalacturonase and pectinesterase were separated from culture filtrates of Trichoderma reesei QM9414 by Sephadex chromatography. Exopolygalacturonase was characterized by specific cleavage of pectic acid to form d-galactopyranuronic acid, and by the hydrolysis of oligomers (highest reaction rate at pentamer). Polygalacturonase exhibited 2 pH-optima peaks (at 4.8 and 5.1) and 10 bands with enzyme activity by isoelectric focusing (IEF) (pI 4.6–8.5). Pectinesterase showed a pH-optimum at 7.6, and 6 enzyme-activity bands on an IEF zymogram which seemed identical with those of higher plants (tomato, alfalfa).
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 7 (1987), S. 425-429 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Intracellular concentrations of ATP, cyclic AMP and glucose-6-phosphate were monitored during growth of partially catabolically derepressed strain of Trichoderma reesei CC II in medium containing lactose as the sole carbon source. The induction of cellulase synthesis occured when the concentration of lactose in the medium decreased below 7 mg/ml. The onset of cellulase synthesis was preceded by a transient peak of intracellular concentration of ATP and by the increase of the cyclic AMP contents in the mycelium whereby the intracellular level of glucose-6-phosphate was at its minimum. By keeping the lactose concentration in the medium at 2 mg/ml, it was possible to support the continuation of cellulase synthesis over the prolonged periods without appreciable growth of biomass.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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