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Trichoderma reesei

About: Trichoderma reesei is a research topic. Over the lifetime, 3832 publications have been published within this topic receiving 152877 citations. The topic is also known as: Trichoderma reesi.


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Journal ArticleDOI
TL;DR: The AT-rich xynB gene of Dictyoglomus thermophilum is reconstructed according to Trichoderma codon preferences and a dramatic increase in expression is demonstrated and a heterologous fungal gene, Humicola grisea xyn2, could be expressed without codon modification.
Abstract: Bulk production of xylanases from thermophilic microorganisms is a prerequisite for their use in industrial processes. As effective secretors of gene products, fungal expression systems provide a promising, industrially relevant alternative to bacteria for heterologous enzyme production. We are currently developing the yeast Kluyveromyces lactis and the filamentous fungus Trichoderma reesei for the extracellular production of thermophilic enzymes for the pulp and paper industry. The K. lactis system has been tested with two thermophilic xylanases and secretes gram amounts of largely pure xylanase A from Dictyoglomus thermophilum in chemostat culture. The T. reesei expression system involves the use of the cellobiohydrolase I (CBHI) promoter and gene fusions for the secretion of heterologous thermostable xylanases of both bacterial and fungal origin. We have reconstructed the AT-rich xynB gene of Dictyoglomus thermophilum according to Trichoderma codon preferences and demonstrated a dramatic increase in expression. A heterologous fungal gene, Humicola grisea xyn2, could be expressed without codon modification. Initial amounts of the XYN2 protein were of a gram per liter range in shake-flask cultivations, and the gene product was correctly processed by the heterologous host. Comparison of the expression of three thermophilic heterologous microbial xylanases in T. reesei demonstrates the need for addressing each case individually.

74 citations

Journal ArticleDOI
TL;DR: This assay could measure, in a onestep method, the initial stages of the degradation of cellulose derivatives by endo-1,4-β-D-glucanases, by determining the reducing end-groups released, and can be extended to the evaluation of reducing groups released by the action of many other carbohydrases, either with Endo- or exo-type activity.
Abstract: It is widely accepted that viscometric assays are the most sensitive methods for evaluation of endoglucanase activities, because of the preferential attack of these enzymes on internal bonds of the substrate. However, due to the high sensitivity of the disodium 2,2′-bicinchoninate assay, we could measure, in a onestep method, the initial stages of the degradation of cellulose derivatives by endo-1,4-β-D-glucanases, by determining the reducing end-groups released. We report the applicability of the method for the determination of activity, and the Km for the endoglucanase-I from Trichoderma reesei. This assay can be extended to the evaluation of reducing groups released by the action of many other carbohydrases, either with endo- or exo-type activity.

74 citations

Journal ArticleDOI
TL;DR: This work has taken a phylogenomic approach to study the PKS repertoire encoded in the genomes of Trichoderma reesei, Trichodma atroviride and Trichodingma virens, and lays a foundation for future research related to PKSs within the genus Trichodyma and in other filamentous fungi.
Abstract: Members of the economically important ascomycete genus Trichoderma are ubiquitously distributed around the world. The mycoparasitic lifestyle and plant defence-inducing interactions of Trichoderma spp. make them ideal biocontrol agents. Of the Trichoderma enzymes that produce secondary metabolites, some of which likely play important roles in biocontrol processes, polyketide synthase (PKSs) have garnered less attention than non-ribosomal peptide synthetases such as those that produce peptaibols. We have taken a phylogenomic approach to study the PKS repertoire encoded in the genomes of Trichoderma reesei, Trichoderma atroviride and Trichoderma virens. Our analysis lays a foundation for future research related to PKSs within the genus Trichoderma and in other filamentous fungi.

74 citations

Journal ArticleDOI
TL;DR: Evaluation and comparison of the specific activities of the enzymes (WT, W40A, and the corresponding catalytic subunits) adsorbed on crystalline cellulose indicated that Trp-40 is involved in recruiting individual substrate chains into the active site tunnel to initiate processive hydrolysis of TrCel7A.

74 citations

Journal ArticleDOI
TL;DR: It is suggested that lactose may function as an inducer for cellulase formation if it is taken up in the mycelium of T. reesei PC-3-7, and that sophorose, cellobiose or galactose may induce a putative lactose permease.
Abstract: In an attempt to clarify the function of lactose in cellulase induction, experiments were carried out on cellulase formation by lactose along with other sugars in a resting cell system of Trichoderma reesei PC-3-7, a hypercellulase-producing mutant. Although lactose alone induces little cellulase under the conditions used, a synergistic effect on cellulase formation was observed following the respective addition of sophorose, cellobiose or galactose to lactose. The lactose consumption was more rapid when these sugars were added than in their absence. Furthermore, following lactose addition 10 h after the beginning of cultivation in the presence of cellobiose, cellulase formation was initiated with only a little lag, and lactose consumption started immediately, being complete in 14 h. \-Galactosidase induction experiments suggested that the rapid consumption of lactose is possibly not dependent on lactose degradation by the enzyme. From these results, it is suggested that lactose may function as an inducer for cellulase formation if it is taken up in the mycelium of T. reesei PC-3-7, and that sophorose, cellobiose or galactose may induce a putative lactose permease. *** DIRECT SUPPORT *** AG903066 00005

74 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202373
2022177
2021134
2020141
2019138
2018142