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: An enzyme-linked immunosorbent assay (ELISA) using monoclonal antibodies has been developed to measure the concentration of three main cellulase components from Trichoderma reesei, cellobiohydrolase I (CBH I) and I (EG I), in both commercial enzyme preparations as well as in samples from laboratory fermentations.
Abstract: An enzyme-linked immunosorbent assay (ELISA) using monoclonal antibodies has been developed to measure the concentration of three main cellulase components from Trichoderma reesei, cellobiohydrolase I (CBH I), cellobiohydrolase II (CBH II) and I (EG I), in both commercial enzyme preparations as well as in samples from laboratory fermentations. The sensitivity of the assay is 1–10 ng protein, depending on the type of cellulase. The coefficient of variability is between 10% and 20%. By a combination of two different domain-specific monoclonals against CBH I or II it is also possible to quantify the concentration of intact and truncated forms of these two enzymes, respectively. The use of the ELISA to quantify the formation of the three cellulase components under different cultivation conditions is described.
56 citations
TL;DR: Subtractive hybridisation was used to target novel genes involved in the mycoparasitic interaction of the biocontrol agent Trichoderma hamatum with the phytopathogen Sclerotinia sclerotiorum, finding some had similarity to known fungal or bacterial genes whereas others had no similarity to any genes previously described.
Abstract: Subtractive hybridisation was used to target novel genes involved in the mycoparasitic interaction of the biocontrol agent Trichoderma hamatum with the phytopathogen Sclerotinia sclerotiorum. Nineteen novel T. hamatum genes were identified that showed increased expression during mycoparasitism compared to a T. hamatum control. Sequence analysis revealed some cDNA fragments had similarity to known fungal or bacterial genes whereas others had no similarity to any genes previously described. Only one of the novel genes has been characterised in another Trichoderma species, the Trichoderma reesei hex1gene. The proteins encoded by the novel genes included three monooxygenases, a metalloendopeptidase, a gluconate dehydrogenase, an endonuclease and a proton ATPase.
56 citations
TL;DR: The cellulosome was tested under varying concentrations of chemical compounds derived from lignocellulose pretreatment and fermentation and exhibited higher ethanol tolerance and thermostability than commercialized fungal (Trichoderma reesei) cellulase.
56 citations
TL;DR: One-step fermentation proved to be a promising strategy for AXOS production from BSG, presenting a performance comparable with the use of commercial enzymes, enabling further developments of low-cost bioprocesses for the production of these valuable compounds.
56 citations
TL;DR: Property related to processivity is compared and the binding affinity changes for mutation of four aromatic residues lining the Cel7A active site tunnel and Cel7B cleft to alanine are computed and the -2 site is similar in both enzymes.
Abstract: In nature, processive and non-processive cellulase enzymes deconstruct cellulose to soluble sugars. From structural studies, the consensus is that processive cellulases exhibit tunnels lined with aromatic and polar residues, whereas non-processive cellulases exhibit open clefts with fewer ligand contacts. To gain additional insight into the differences between processive and non-processive cellulases, we examine the glycoside hydrolase family 7 (GH7) cellobiohydrolase, Cel7A, and the endoglucanase, Cel7B, from Trichoderma reesei with molecular simulation. We compare properties related to processivity and compute the binding affinity changes for mutation of four aromatic residues lining the Cel7A active site tunnel and Cel7B cleft to alanine. For the wild-type enzymes, dissimilar behavior is observed at nearly every glucopyranose-binding site from −7 to +2, except in the −2 site, suggesting that the structural differences directly around the catalytic center and at the active site tunnel entrances and exit...
55 citations