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 1,4-β-D-glucan cellobiohydrolase I (CBHI) from Trichoderma reesei was labelled with 4-6 nm gold particles as discussed by the authors.
124 citations
TL;DR: The production of both homologous and heterologous proteins with the cellulolytic filamentous fungus Trichoderma reesei and the expression and secretion of active calf chymosin is described in detail.
123 citations
TL;DR: This work probes the molecular-level behavior of the Family 1 carbohydrate-binding module (CBM) from a commonly studied fungal cellulase, the Family 7 cellobiohydrolase (Cel7A) from Trichoderma reesei, on the hydrophobic face of crystalline cellulose to imply that the CBM can anchor the Cel7A enzyme at discrete points along a cellulose chain and thus aid in both recognizing celluloseChain ends for initial attachment to
Abstract: We probe the molecular-level behavior of the Family 1 carbohydrate-binding module (CBM) from a commonly studied fungal cellulase, the Family 7 cellobiohydrolase (Cel7A) from Trichoderma reesei, on the hydrophobic face of crystalline cellulose. With a fully atomistic model, we predict that the CBM alone exhibits regions of thermodynamic stability along a cellulose chain corresponding to a cellobiose unit, which is the catalytic product of the entire Cel7A enzyme. In addition, we determine which residues and the types of interactions that are responsible for the observed processivity length scale of the CBM: Y5, Q7, N29, and Y32. These results imply that the CBM can anchor the Cel7A enzyme at discrete points along a cellulose chain and thus aid in both recognizing cellulose chain ends for initial attachment to cellulose as well as aid in enzymatic catalysis by diffusing between stable wells on a length scale commensurate with the catalytic, processive cycle of Cel7A during cellulose hydrolysis. Comparison o...
123 citations
TL;DR: In the present study, Trichoderma reesei cellulase was covalently immobilized on chitosan-coated magnetic nanoparticles using glutaraldehyde as a coupling agent to reduce the enzyme consumption during lignocellulosic material saccharification for bioethanol production.
Abstract: In the present study, Trichoderma reesei cellulase was covalently immobilized on chitosan-coated magnetic nanoparticles using glutaraldehyde as a coupling agent. The average diameter of magnetic nanoparticles before and after enzyme immobilization was about 8 and 10 nm, respectively. The immobilized enzyme retained about 37 % of its initial activity, and also showed better thermal and storage stability than free enzyme. Immobilized cellulase retained about 80 % of its activity after 15 cycles of carboxymethylcellulose hydrolysis and was easily separated with the application of an external magnetic field. However, in this reaction, K
m was increased eight times. The immobilized enzyme was able to hydrolyze lignocellulosic material from Agave atrovirens leaves with yield close to the amount detected with free enzyme and it was re-used in vegetal material conversion up to four cycles with 50 % of activity decrease. This provides an opportunity to reduce the enzyme consumption during lignocellulosic material saccharification for bioethanol production.
123 citations
TL;DR: In this article, the optimal arabinose-releasing and xylan-depolymerizing enzyme activities were identified from data obtained when selected, recombinant enzymes were systematically supplemented to the different arabinoxylan substrates in mixtures.
Abstract: This study describes the identification of the key enzyme activities required in a "minimal" enzyme cocktail able to catalyze hydrolysis of water-soluble and water-insoluble wheat arabinoxylan and whole vinasse, a fermentation effluent resulting from industrial ethanol manufacture from wheat. The optimal arabinose-releasing and xylan-depolymerizing enzyme activities were identified from data obtained when selected, recombinant enzymes were systematically supplemented to the different arabinoxylan substrates in mixtures; this examination revealed three novel alpha-l-arabinofuranosidase activities: (i) one GH51 enzyme from Meripilus giganteus and (ii) one GH51 enzyme from Humicola insolens, both able to catalyze arabinose release from singly substituted xylose; and (iii) one GH43 enzyme from H. insolens able to catalyze the release of arabinose from doubly substituted xylose. Treatment of water-soluble and water-insoluble wheat arabinoxylan with an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-l-arabinofuranosidase from H. insolens (Abf II), the GH51 alpha-l-arabinofuranosidase from M. giganteus (Abf III), a GH10 endo-1,4-beta-xylanase from H. insolens (Xyl III), and a GH3 beta-xylosidase from Trichoderma reesei (beta-xyl) released 322 mg of arabinose and 512 mg of xylose per gram of water-soluble wheat arabinoxylan dry matter and 150 mg of arabinose and 266 mg of xylose per gram of water-insoluble wheat arabinoxylan dry matter after 24 h at pH 5, 50 degrees C. A 10%:40%:50% mixture of Abf II, Abf III, and beta-xyl released 56 mg of arabinose and 91 mg of xylose per gram of vinasse dry matter after 24 h at pH 5, 50 degrees C. The optimal dosages of the "minimal" enzyme cocktails were determined to be 0.4, 0.3, and 0.2 g enzyme protein per kilogram of substrate dry matter for the water-soluble wheat arabinoxylan, the water-insoluble wheat arabinoxylan, and the vinasse, respectively. These enzyme protein dosage levels were approximately 14, approximately 18, and approximately 27 times lower than the dosages used previously, when the same wheat arabinoxylan substrates were hydrolyzed with a combination of Ultraflo L and Celluclast 1.5 L, two commercially available enzyme preparations produced by H. insolens and T. reesei.
123 citations