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Riin Kont
University of Tartu
Substrate (chemistry)CellulaseTrichoderma reeseiCelluloseBiochemistry
7Publications
4H-index
103Citations
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Publications 7
Newest
#1Josh V. VermaasH-Index: 12
#2Riin KontH-Index: 4
Last. Brandon C. KnottH-Index: 13
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#1Josh V. Vermaas (NREL: National Renewable Energy Laboratory)H-Index: 12
#2Riin Kont (UT: University of Tartu)H-Index: 4
Last. Brandon C. Knott (NREL: National Renewable Energy Laboratory)H-Index: 13
view all 9 authors...
Cellulase enzymes deconstruct recalcitrant cellulose into soluble sugars, making them a biocatalyst of biotechnological interest for use in the nascent lignocellulosic bioeconomy. Cellobiohydrolases (CBHs) are cellulases capable of liberating many sugar molecules in a processive manner without dissociating from the substrate. Within the complete processive cycle of CBHs, dissociation from the cellulose substrate is rate limiting, but the molecular mechanism of this step is unknown. Here, we pres...
3 CitationsSource
#1Riin Kont (UT: University of Tartu)H-Index: 4
#2Ville Pihlajaniemi (VTT Technical Research Centre of Finland)H-Index: 11
Last. Priit Väljamäe (UT: University of Tartu)H-Index: 20
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Background Enzyme-aided valorization of lignocellulose represents a green and sustainable alternative to the traditional chemical industry. The recently discovered lytic polysaccharide monooxygenases (LPMOs) are important components of the state-of-the art enzyme cocktails for cellulose conversion. Yet, these monocopper enzymes are poorly characterized in terms of their kinetics, as exemplified by the growing evidence for that H2O2 may be a more efficient co-substrate for LPMOs than O2. LPMOs ne...
Source
#1Silja KuuskH-Index: 9
#2Riin KontH-Index: 4
Last. Priit VäljamäeH-Index: 20
view all 8 authors...
: Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes that catalyze oxidative cleavage of glycosidic bonds in polysaccharides in the presence of an external electron donor (reductant). In the classical O2-driven monooxygenase reaction, the reductant is needed in stoichiometric amounts. In a recently discovered, more efficient H2O2-driven reaction, the reductant would be needed only for the initial reduction (priming) of the LPMO to its catalytically active Cu(I) form. However, the...
11 CitationsSource
#1Jeppe KariH-Index: 9
#2Riin Kont (UT: University of Tartu)H-Index: 4
Last. Peter WesthH-Index: 38
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Cellobiohydrolases (CBHs) make up an important group of enzymes for both natural carbon cycling and industrial deconstruction of lignocellulosic biomass. The consecutive hydrolysis of one cellulose strand relies on an intricate pattern of enzyme–substrate interactions in the long, tunnel-shaped binding site of the CBH. In this work, we have investigated the initial complexation mode with cellulose of the most thoroughly studied CBH, Cel7A from Hypocrea jecorina (HjCel7A). We found that HjCel7A p...
5 CitationsSource
#1Riin Kont (UT: University of Tartu)H-Index: 4
#2Jeppe Kari (RU: Roskilde University)H-Index: 9
Last. Priit Väljamäe (UT: University of Tartu)H-Index: 20
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Abstract Structural polysaccharides like cellulose and chitin are abundant and their enzymatic degradation to soluble sugars is an important route in green chemistry. Processive glycoside hydrolases (GHs), like cellobiohydrolase Cel7A of Trichoderma reesei (TrCel7A) are key components of efficient enzyme systems. TrCel7A consists of a catalytic domain (CD) and a smaller carbohydrate-binding module (CBM) connected through the glycosylated linker peptide. A tunnel-shaped active site rests in the C...
19 CitationsSource
#1Riin Kont (UT: University of Tartu)H-Index: 4
#2Mihhail Kurašin (UT: University of Tartu)H-Index: 5
Last. Priit Väljamäe (UT: University of Tartu)H-Index: 20
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Background The use of the enzymatic hydrolysis of lignocellulose with subsequent fermentation to ethanol provides a green alternative for the production of transportation fuels. Because of its recalcitrant nature, the lignocellulosic biomass must be pretreated before enzymatic hydrolysis. However, the pretreatment often results in the formation of compounds that are inhibitory for the enzymes or fermenting organism. Although well recognized, little quantitative information on the inhibition of i...
65 CitationsSource
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