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: Indications of hetero-cross-link formation between alpha-casein and hOSX by both oxidative enzymes could be visualized by glycoprotein-specific staining in the SDS-PAGE analysis, although ThL was observed to be more effective in the heteroconjugate formation than TrT.
Abstract: Proteins and certain carbohydrates contain phenolic moieties, which are potential sites for modification of the function of the biopolymers In this study, the capability of two different fungal oxidative enzymes, laccase from Trametes hirsuta (ThL) and tyrosinase from Trichoderma reesei (TrT), to catalyze formation of hetero-cross-linking between tyrosine side chains of α-casein and phenolic acids of hydrolyzed oat spelt xylan (hOSX) was studied Formation of reaction products was followed by size exclusion chromatography (SEC), fluorescence spectroscopy, and SDS-PAGE, using specific staining methods for proteins and protein−carbohydrate conjugates ThL and TrT were observed to differ significantly in their ability to catalyze the formation of protein−carbohydrate conjugates or the linking of the small molecular weight phenolic compounds to α-casein The efficiency of these enzymes to directly cross-link protein also differed notably TrT was able to cross-link α-casein more efficiently than ThL ThL-cat
132 citations
TL;DR: Electrophoretic mobility shift assays, using cell-free extracts, identified induction-specific protein-DNA complexes: one complex of high mobility was observed under basal, noninduced conditions (glucose) with xyn2, which was in part replaced by a slow-migrating complex upon induction by xylan or sophorose.
132 citations
TL;DR: In this article, the effects of fermentation parameters for cellulase production by Trichoderma reesei QM9414 and T.Reesei MCG77 in solid-state fermentation using rice bran as substrate were evaluated.
132 citations
TL;DR: The endoglucanase activity produced by the EGII transformants correlated with the copy number of the egl2 expression cassette, and an improved stonewashing effect on denim fabric was achieved when the enzyme with elevated EGII content was used.
Abstract: Trichoderma reesei strains were constructed for production of elevated amounts of endoglucanase II (EGII) with or without cellobiohydrolase I (CBHI). The endoglucanase activity produced by the EGII transformants correlated with the copy number of the egl2 expression cassette. One copy of the egl2 expression cassette in which the egl2 was under the cbh1 promoter increased production of endoglucanase activity 2.3-fold, and two copies increased production about 3-fold above that of the parent strain. When the enzyme with elevated EGII content was used, an improved stonewashing effect on denim fabric was achieved. A T. reesei strain producing high amounts of EGI and -II activities without CBHI and -II was constructed by replacing the cbh2 locus with the coding region of the egl2 gene in the EGI-overproducing CBHI-negative strain. Production of endoglucanase activity by the EG-transformant strain was increased fourfold above that of the host strain. The filter paper-degrading activity of the endoglucanase-overproducing strain was lowered to below detection, presumably because of the lack of cellobiohydrolases.
131 citations
TL;DR: The resulting models show a “tadpole”-like structure for the intact enzyme where the isotropic part coincides with the core protein and the flexible tail part should be identified with the C-terminal glycopeptide.
Abstract: Limited proteolysis (papain) of the cellobiohydrolase I (CBH I, 65 kDa) from Trichoderma reesei led to the seperation of two functional domains: a core protein (55 kDa) containing the active site, and a C-terminal glycopeptide (10 kDa) implicated in binding to the insoluble matrix (cellulose). The quaternary structures of the intact CBH I and its core in solution are now compared by small angle X-ray scattering (SAXS) measurements. The molecular parameters derived for the core (Rg=2.09 nm, Dmax=6.5 nm) and for the intact enzyme (Rg=4.27 nm, Dmax=18 nm) indicate very different shapes. The resulting models show a “tadpole”-like structure for the intact enzyme where the isotropic part coincides with the core protein and the flexible tail part should be identified with the C-terminal glycopeptide. Thus in this enzyme, functional differentiation is reflected in structural peculiarities.
131 citations