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: A cDNA encoding 1,2-α- d -mannosidase mds1 from Trichoderma reesei was cloned and the enzymatic properties were analysed and the enzyme was characterized as a class-I mannosidase.
102 citations
TL;DR: In this paper, the effects of swollenin on cellulosic particle size, maximum cellulase adsorption and cellulose crystallinity were quantified for the first time and were comparable to those of individual cellulases from T. reesei.
Abstract: In order to generate biofuels, insoluble cellulosic substrates are pretreated andsubsequently hydrolyzed with cellulases. One way to pretreat cellulose in a safeand environmentally friendly manner is to apply, under mild conditions,non-hydrolyzing proteins such as swollenin - naturally produced in low yields bythe fungus Trichoderma reesei. To yield sufficient swollenin forindustrial applications, the first aim of this study is to present a new way ofproducing recombinant swollenin. The main objective is to show how swolleninquantitatively affects relevant physical properties of cellulosic substrates andhow it affects subsequent hydrolysis. After expression in the yeast Kluyveromyces lactis, the resultingswollenin was purified. The adsorption parameters of the recombinant swolleninonto cellulose were quantified for the first time and were comparable to those ofindividual cellulases from T. reesei. Four different insoluble cellulosicsubstrates were then pretreated with swollenin. At first, it could bequalitatively shown by macroscopic evaluation and microscopy that swollenin causeddeagglomeration of bigger cellulose agglomerates as well as dispersion ofcellulose microfibrils (amorphogenesis). Afterwards, the effects of swollenin oncellulose particle size, maximum cellulase adsorption and cellulose crystallinitywere quantified. The pretreatment with swollenin resulted in a significantdecrease in particle size of the cellulosic substrates as well as in theircrystallinity, thereby substantially increasing maximum cellulase adsorption ontothese substrates. Subsequently, the pretreated cellulosic substrates werehydrolyzed with cellulases. Here, pretreatment of cellulosic substrates withswollenin, even in non-saturating concentrations, significantly accelerated thehydrolysis. By correlating particle size and crystallinity of the cellulosicsubstrates with initial hydrolysis rates, it could be shown that theswollenin-induced reduction in particle size and crystallinity resulted in highcellulose hydrolysis rates. Recombinant swollenin can be easily produced with the robust yeast K.lactis. Moreover, swollenin induces deagglomeration of celluloseagglomerates as well as amorphogenesis (decrystallization). For the first time,this study quantifies and elucidates in detail how swollenin affects differentcellulosic substrates and their hydrolysis.
102 citations
TL;DR: This study compares the capacity for coproduction of nanocellulose and fermentable sugars using two vastly different cellulase systems: the classical "free enzyme" system of the saprophytic fungus, Trichoderma reesei, and the complexed, multifunctional enzymes produced by the hot springs resident, Caldicellulosiruptor bescii.
Abstract: Producing fuels, chemicals, and materials from renewable resources to meet societal demands remains an important step in the transition to a sustainable, clean energy economy. The use of cellulolytic enzymes for the production of nanocellulose enables the coproduction of sugars for biofuels production in a format that is largely compatible with the process design employed by modern lignocellulosic (second generation) biorefineries. However, yields of enzymatically produced nanocellulose are typically much lower than those achieved by mineral acid production methods. In this study, we compare the capacity for coproduction of nanocellulose and fermentable sugars using two vastly different cellulase systems: the classical “free enzyme” system of the saprophytic fungus, Trichoderma reesei (T. reesei) and the complexed, multifunctional enzymes produced by the hot springs resident, Caldicellulosiruptor bescii (C. bescii). We demonstrate by comparative digestions that the C. bescii system outperforms the fungal ...
101 citations
TL;DR: Some aspects of the chromosomal organization, structure, and transcription of these genes are unlike those of any previously described cellulase genes.
Abstract: Restriction mapping and sequence analysis of cosmid clones revealed a cluster of three cellobiohydrolase genes in Phanerochaete chrysosporium P chrysosporium cbh1-1 and cbh1-2 are separated by only 750 bp and are located approximately 14 kb upstream from a cellulase gene previously cloned from P chrysosporium (P Sims, C James, and P Broda, Gene 74:411-422, 1988) Within a well-conserved region, the deduced amino acid sequences of P chrysosporium cbh1-1 and cbh1-2 are, respectively, 80 and 69% homologous to that of the Trichoderma reesei cellobiohydrolase I gene The conserved cellulose-binding domain typical of microbial cellulases is absent from cbh1-1 Transcript levels of the three P chrysosporium genes varied substantially, depending on culture conditions cbh1-1 and cbh1-2 were not induced in the presence of cellulose, nor did they appear to be subject to glucose repression Therefore, aspects of the chromosomal organization, structure, and transcription of these genes are unlike those of any previously described cellulase genes
101 citations
TL;DR: Binding experiments using activity detection of Man5A and Man5ADeltaCBM suggests that the CBM binds to cellulose but not to mannan, which is closely associated with cellulose in plant cell walls.
101 citations