Topic
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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TL;DR: The recombinant enzyme expresses a gene encoding the ligninolytic laccase enzyme of the white–rot fungus Phlebia radiata in the soft rot fungus Trichoderma reesei and is analogous to thePhlebia enzyme in removing monomeric lignin–related compounds from residualLignin of the pulping process, thus demonstrating its potential for industrial applications.
Abstract: We have expressed a gene encoding the ligninolytic laccase enzyme of the white–rot fungus Phlebia radiata in the soft rot fungus Trichoderma reesei under the promoter of the major cellulase gene (cbh1). Constructions from the laccase cDNA or the chromosomal gene were equivalent in expression, yielding 20 mg/l of secreted active laccase in small–scale fermentations. The recombinant enzyme has a similar molecular weight, antigenic properties and specific activity as the Phlebia laccase and is analogous to the Phlebia enzyme in removing monomeric lignin–related compounds from residual lignin of the pulping process, thus demonstrating its potential for industrial applications.
103 citations
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TL;DR: Reaction patterns for the hydrolysis of chromophoric glycosides from cello-oligosaccharides and lactose by the cellobiohydrolases purified from Trichoderma reesei and Penicillium pinophilum were determined.
Abstract: Reaction patterns for the hydrolysis of chromophoric glycosides from cello-oligosaccharides and lactose by the cellobiohydrolases (CBH I and CBH II) purified from Trichoderma reesei and Penicillium pinophilum were determined. They coincide with those found for the parent unsubstituted sugars. CBH I enzyme from both organisms attacks these substrates in a random manner. Turnover numbers are, however, low and do not increase appreciably as a function of the degree of polymerization of the substrates. The active-site topology of the CBH I from T. reesei was further probed by equilibrium binding experiments with cellobiose, cellotriose, lactose and some of their derivatives. These point to a single interaction site (ABC), spatially restricted as deduced from the apparent independency of the thermodynamic parameters. It appears that the putative subsite A can accommodate a galactopyranosyl or glucopyranosyl group, and subsite B a glucopyranosyl group, whereas in subsite C either a glucopyranosyl or a chromophoric group can be bound, scission occurring between subsites B and C. The apparent kinetic parameters (turnover numbers) for the hydrolysis of cello-oligosaccharides (and their derivatives) by the CBH II type enzyme increase as a function of chain length, indicative of an extended binding site (A-F). Its architecture allows for specific binding of beta-(1----4)-glucopyranosyl groups in subsites A, B and C. Binding of a chromophore in subsite C produces a non-hydrolysable complex. The thermodynamic interaction parameters of some ligands common to both type of enzyme were compared: these substantiate the conclusions reached above.
103 citations
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TL;DR: The normal glycosylation pattern of CBH I, the major glycoprotein secreted by Trichoderma reesei, has been characterized and it may be possible to use T.Reesei as a host for the production of heterologous glycoproteins of animal origin, and to take advantage of its remarkable secretory capacity.
Abstract: With the object of obtaining information about the suitability of filamentous fungi for production of heterogeneous mammalian proteins, we have characterized the normal glycosylation pattern of CBH I, the major glycoprotein secreted by Trichoderma reesei. The protein–bound glycans of CBH I were studied using a variety of separation techniques to analyze the products of specific glycosidase digestions and chemical degradation procedures. CBH I contains both O–glycosidic and N–glycosidic glycans. The O–glycosidic glycans consist of one to four hexose residues which are mostly mannose. The structures of the N–glycosidic glycans are (Man)5(GlcNAc)2 and (Man)9(GlcNAc)2. Thus it may be possible to use T. reesei as a host for the production of heterologous glycoproteins of animal origin, and to take advantage of its remarkable secretory capacity.
103 citations
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TL;DR: This work has identified every site of glycosylation of CBHI from a high cellulase-producing mutant strain of T. reesei, ALKO2877, and characterised each site in terms of its modifying carbohydrate and site-specific heterogeneity.
102 citations
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TL;DR: Deletion of vel1 completely impaired the expression of cellulases, xylanases and the cellulase regulator XYR1 on lactose as a cellulase inducing carbon source, but also in resting mycelia with sophorose as inducer.
Abstract: Trichoderma reesei is the industrial producer of cellulases and hemicellulases for biorefinery processes. Their expression is obligatorily dependent on the function of the protein methyltransferase LAE1. The Aspergillus nidulans orthologue of LAE1 - LaeA - is part of the VELVET protein complex consisting of LaeA, VeA and VelB that regulates secondary metabolism and sexual as well as asexual reproduction. Here we have therefore investigated the function of VEL1, the T. reesei orthologue of A. nidulans VeA. Deletion of the T. reesei vel1 locus causes a complete and light-independent loss of conidiation, and impairs formation of perithecia. Deletion of vel1 also alters hyphal morphology towards hyperbranching and formation of thicker filaments, and with consequently reduced growth rates. Growth on lactose as a sole carbon source, however, is even more strongly reduced and growth on cellulose as a sole carbon source eliminated. Consistent with these findings, deletion of vel1 completely impaired the expression of cellulases, xylanases and the cellulase regulator XYR1 on lactose as a cellulase inducing carbon source, but also in resting mycelia with sophorose as inducer. Our data show that in T. reesei VEL1 controls sexual and asexual development, and this effect is independent of light. VEL1 is also essential for cellulase gene expression, which is consistent with the assumption that their regulation by LAE1 occurs by the VELVET complex.
102 citations