Results 171 to 180 of about 21,091 (214)

Enzyme production by recombinant Trichoderma reesei strains

Journal of Biotechnology, 1991
The production of both homologous and heterologous proteins with the cellulolytic filamentous fungus Trichoderma reesei is described. Biotechnically important improvements in the production of cellulolytic enzymes have been obtained by genetic engineering methodology to construct strains secreting novel mixtures of cellulases.
Uusitalo, Jaana M., Helena Nevalainen, K. M., Harkki, Anu M., Knowles, Jonathan K.C., Penttilä, Merja E.   +4 more
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RNA Characterization in Trichoderma reesei

2020
This chapter provides an overview on different methods for the characterization of RNAs in Trichoderma reesei. In the first section, protocols for the extraction of total RNA from fungal mycelia and the identification of 5' and 3' ends of certain RNAs of interest via rapid amplification of cDNA ends (RACE) are presented.
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Chitinous Material in Trichoderma reesei

Biotechnology Letters, 1998
Trichoderma reesei was grown for 180h in batch culture in an 8 liter stirred fermenter using a glucose-rich medium. Concentrations of glucose, ammonia, cell dry weight, debris and lipid are presented for two runs. Cell dry weights reached 26.9g/L and 19.6g/L in these runs.
D.E. Brown, A.J. Thornton
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Sexual Crossing of Trichoderma reesei

2020
This chapter describes how mating assays in Trichoderma reesei can successfully be performed and which specific prerequisites of industrial strains originating from strain QM6a have to be met for successful mating experiments.
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Cellulose hydrolysis by immobilized Trichoderma reesei cellulase

Biotechnology Letters, 2009
Cellulose hydrolysis by immobilized Trichoderma reesei cellulase in the presence of a low viscosity ionic liquid, 1-ethyl-3-methylimidazolium diethyl phosphate (EMIM-DEP), was investigated. Preparation of the carrier-free immobilized cellulase was optimized with respect to concentration of the cross-linker and the type of precipitant. The addition of 2%
Paetrice O, Jones, Palligarnai T, Vasudevan   +1 more
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Two major xylanases of Trichoderma reesei

Enzyme and Microbial Technology, 1992
The two main xylanases produced by Trichoderma reesei were purified to electrophoretic homogeneity by ion-exchange and gel chromatography. The enzymes had isoelectric points of 9.0 and 5.5 and their molecular masses were 20 and 19 kDa, respectively.
Tenkanen, Maija, Puls, Jurgen, Poutanen, Kaisa   +2 more
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Ecological Genomics and Evolution of Trichoderma reesei

2020
The filamentous fungus Trichoderma reesei (Hypocreales, Ascomycota) is an efficient industrial cell factory for the production of cellulolytic enzymes used for biofuel and other applications. Therefore, researches addressing T. reesei are relatively advanced compared to other Trichoderma spp.
Komal, Chenthamara, Irina S, Druzhinina, Mohammad J, Rahimi, Marica, Grujic, Feng, Cai   +4 more
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Characterization of the Trichoderma reesei cbh2 promoter

Current Genetics, 1993
A 613-bp fragment of the 5' upstream region of the Trichoderma reesei cbh2 gene (coding for the cellulolytic enzyme cellobiohydrolase II) has been isolated and sequenced. Fusion of this fragment to the E. coli uidA gene (coding for beta-glucuronidase) leads to--albeit low--expression of beta-glucuronidase activity in the presence of cellulose and upon ...
H, Stangl, F, Gruber, C P, Kubicek
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Glucose-induced secretion of Trichoderma reesei xylanases

Applied and Environmental Microbiology, 1996
To produce two xylanases with Trichoderma reesei grown on glucose, recombinant strains which carry either the xyn1 or the xyn2 (xylanase I and II [XYN I and XYN II]-encoding) structural genes under the expression signals of the homologous pki1 (pyruvate kinase-encoding) gene were constructed.
W, Kurzatkowski, A, Törrönen, J, Filipek, R L, Mach, P, Herzog, S, Sowka, C P, Kubicek   +6 more
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Domain function in Trichoderma reesei cellobiohydrolases

Journal of Biotechnology, 1992
The filamentous fungus, Trichoderma reesei produces all of the enzymatic activities required for efficient hydrolysis of highly ordered crystalline cellulose. All the principal enzymes involved in cellulose hydrolysis possess two functional domains, one directly involved in catalysis and the other in substrate recognition and binding.
Teeri, Tuula, Reinikainen, Tapani, Ruohonen, Laura, Jones, Alwyn, Knowles, Jonathan   +4 more
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