about
Multi-mode binding of Cellobiohydrolase Cel7A from Trichoderma reesei to cellulose.Human Chitotriosidase Is an Endo-Processive Enzyme.When substrate inhibits and inhibitor activates: implications of β-glucosidases.Anomeric Selectivity and Product Profile of a Processive Cellulase.Thermodynamic Relationships with Processivity in Serratia marcescens Family 18 Chitinases.Processivity of cellobiohydrolases is limited by the substrate.Strong cellulase inhibitors from the hydrothermal pretreatment of wheat straw.Endo-exo synergism in cellulose hydrolysis revisited.Selecting β-glucosidases to support cellulases in cellulose saccharification.Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate.Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.Kinetics of H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase.A pyranose dehydrogenase-based biosensor for kinetic analysis of enzymatic hydrolysis of cellulose by cellulases.Yeast mitochondrial DNA polymerase is a highly processive single-subunit enzyme.Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase IMechanism of substrate inhibition in cellulose synergistic degradationSurface character of pulp fibres studied using endoglucanasesMeasuring processivityMechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysisEnzyme processivity changes with the extent of recalcitrant polysaccharide degradationKinetic insights into the role of the reductant in H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenaseThe liquid fraction from hydrothermal pretreatment of wheat straw provides lytic polysaccharide monooxygenases with both electrons and H2O2 co-substrateThe dissociation mechanism of processive cellulasesThermodynamic Signatures of Substrate Binding for Three Thermobifida fusca Cellulases with Different Modes of Action
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description
researcher ORCID ID = 0000-0002-1035-9493
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wetenschapper
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name
Priit Väljamäe
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Priit Väljamäe
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Priit Väljamäe
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Priit Väljamäe
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Priit Väljamäe
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Priit Väljamäe
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prefLabel
Priit Väljamäe
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Priit Väljamäe
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Priit Väljamäe
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P31
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0000-0002-1035-9493