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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.


Papers
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Journal ArticleDOI
TL;DR: DNA sequencing revealed significant homology at the amino acid level between EGI and exocellobiohydrolase I, but there are differences in codon utilization at homologous amino acids and in the intron/exon structure that possibly reflect a mechanism for preventing recombination between closely related genes of the cellulase family.
Abstract: Cloning, Characterization, and Expression in Saccharomyces Cerevisiae of Endoglucanase I from Trichoderma Reesei

166 citations

Patent
05 Jun 1995
TL;DR: In this article, a process for expressing extracellular β-glucosidase in a filamentous fungus by expressing a fungal DNA sequence encoding enhanced, deleted or altered β glucosidases in a recombinant host microorganism is disclosed.
Abstract: A process for expressing extracellular β-glucosidase in a filamentous fungus by expressing a fungal DNA sequence encoding enhanced, deleted or altered β-glucosidase in a recombinant host microorganism is disclosed. Recombinant fungal cellulase compositions containing enhanced, deleted or altered expression of β-glucosidase is also disclosed.

166 citations

Journal ArticleDOI
TL;DR: Investigation of the effect of acetyl xylan esterase (AXE) originating from Trichoderma reesei on xylan solubilization and enzymatic hydrolysis of cellulose demonstrates that supplementation of xylanase with AXE enhances the solubILization of Xylan to some extent and, consequently, increases the subsequent hydrolytic extent of cellulOSE.
Abstract: Background Due to the complexity of lignocellulosic materials, a complete enzymatic hydrolysis into fermentable sugars requires a variety of cellulolytic and xylanolytic enzymes. Addition of xylanases has been shown to significantly improve the performance of cellulases and to increase cellulose hydrolysis by solubilizing xylans in lignocellulosic materials. The goal of this work was to investigate the effect of acetyl xylan esterase (AXE) originating from Trichoderma reesei on xylan solubilization and enzymatic hydrolysis of cellulose.

165 citations

Journal ArticleDOI
TL;DR: The results for the structural and functional properties of these three β-glucosidases from various biological sources open important avenues of exploration for further practical applications.

164 citations

Journal ArticleDOI
TL;DR: Recovery of high levels of enzyme in T2 ears demonstrated that expression is likely to be stable over multiple generations, and the enzymes were active in cleaving soluble substrate.
Abstract: Ethanol from lignocellulosic biomass is being pursued as an alternative to petroleum-based transportation fuels. To succeed in this endeavour, efficient digestion of cellulose into monomeric sugar streams is a key step. Current production systems for cellulase enzymes, i.e. fungi and bacteria, cannot meet the cost and huge volume requirements of this commodity-based industry. Transgenic maize (Zea mays L.) seed containing cellulase protein in embryo tissue, with protein localized to the endoplasmic reticulum, cell wall or vacuole, allows the recovery of commercial amounts of enzyme. E1 cellulase, an endo-beta-1,4-glucanase from Acidothermus cellulolyticus, was recovered at levels greater than 16% total soluble protein (TSP) in single seed. More significantly, cellobiohydrolase I (CBH I), an exocellulase from Trichoderma reesei, also accumulated to levels greater than 16% TSP in single seed, nearly 1000-fold higher than the expression in any other plant reported in the literature. The catalytic domain was the dominant form of E1 that was detected in the endoplasmic reticulum and vacuole, whereas CBH I holoenzyme was present in the cell wall. With one exception, individual transgenic events contained single inserts. Recovery of high levels of enzyme in T2 ears demonstrated that expression is likely to be stable over multiple generations. The enzymes were active in cleaving soluble substrate.

164 citations


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