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: Using EST analysis and cDNA microarrays, it is found that in Trichoderma reesei expression of the genes encoding the enzymes of the tricarboxylic acid cycle and the proteins of the electron transport chain is programmed in a way that favors the oxidation of pyruvate via the transexual acid cycle rather than its reduction to ethanol by fermentation.
148 citations
TL;DR: The esterase acted in synergism with other xylanolytic enzymes, which was reflected in increased production of phenolic acids from wheat straw xylo-oligosaccharides in the presence of xylanases of Trichoderma reesei.
148 citations
TL;DR: The essential lignocellulolytic proteins for designing an enzyme mixture for optimal lignOcellulosic biomass hydrolysis are discussed here.
148 citations
TL;DR: Trichoderma reesei was co-cultured with Aspergillus phoenicis using dairy manure as a substrate to produce cellulase with a high level of β-glucosidase as discussed by the authors.
147 citations
TL;DR: The kinetics of enzymatic hydrolysis of pure insoluble cellulose by means of unpurified culture filtrate of Trichoderma reesei was studied, and the result has shown that the action of β‐glucosidase is competitively inhibited by glucose.
Abstract: The kinetics of enzymatic hydrolysis of pure insoluble cellulose by means of unpurified culture filtrate of Trichoderma reesei was studied, emphasizing the kinetic characteristics associated with the extended hydrolysis times. The changes in the hydrolysis rate and extent of soluble protein adsorption during the progress of reaction, either apparent or intrinsic, were investigated. The hydrolysis rate declined drastically during the initial hours of hydrolysis. The factors causing the reduction in the hydrolysis rate were examined; these include the transformation of cellulose into a less digestible form and product inhibition. The structural transformation can be partially explained by changes in the crystallinity index and surface area. The product inhibition was caused by the deactivation of the adsorbed soluble protein by the products, which essentially represents the so-called "un-competitive" inhibition. The kinetics of beta-glucosidase were also studied. The result has shown that the action of beta-glucosidase is competitively inhibited by glucose. It has been found that the integrated form of the initial rate expression cannot be used in predicting the progress of reaction because the digestibility of cellulose changes drastically as the hydrolysis proceeds, and that the rate expression for enzymatic hydrolysis of cellulose cannot be simplified or approximated by resorting to the pseudo-steady-state assumption. A mechanistic kinetic model of cellulose hydrolysis should include the following major influencing factors: (1)mode of action of enzyme, (2) structure of cellulose, and (3) mode of interaction between the enzyme and cellulose molecules.
146 citations