Lista de obras -

A pyranose dehydrogenase-based biosensor for kinetic analysis of enzymatic hydrolysis of cellulose by cellulases

artículo científico publicado en 2014

Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I

scientific article published on 01 December 1999

Anomeric Selectivity and Product Profile of a Processive Cellulase

artículo científico publicado en 2016

Endo-exo synergism in cellulose hydrolysis revisited.

artículo científico publicado en 2012

Enzyme processivity changes with the extent of recalcitrant polysaccharide degradation

scientific article published on 05 November 2014

Human Chitotriosidase Is an Endo-Processive Enzyme

artículo científico publicado en 2017

Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate.

artículo científico publicado en 2004

Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.

artículo científico publicado en 2016

Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

artículo científico publicado en 2020

Kinetic insights into the role of the reductant in H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase

artículo científico publicado en 2018

Kinetics of H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase

artículo científico publicado en 2017

Measuring processivity

scientific article published on 01 January 2012

Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis

artículo científico publicado en 2010

Mechanism of substrate inhibition in cellulose synergistic degradation

scientific article published on 01 August 2001

Multi-mode binding of Cellobiohydrolase Cel7A from Trichoderma reesei to cellulose

artículo científico publicado en 2014

Processivity of cellobiohydrolases is limited by the substrate.

artículo científico publicado en 2010

Selecting β-glucosidases to support cellulases in cellulose saccharification.

artículo científico publicado en 2013

Strong cellulase inhibitors from the hydrothermal pretreatment of wheat straw

artículo científico publicado en 2013

Surface character of pulp fibres studied using endoglucanases

artículo científico publicado en 2005

The dissociation mechanism of processive cellulases

artículo científico publicado en 2019

The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface − erosion model ⬇️

artículo científico publicado el 15 de abril de 1998

The liquid fraction from hydrothermal pretreatment of wheat straw provides lytic polysaccharide monooxygenases with both electrons and H2O2 co-substrate

scientific article published on 08 October 2019

Thermodynamic Relationships with Processivity in Serratia marcescens Family 18 Chitinases.

artículo científico

Thermodynamic Signatures of Substrate Binding for Three Thermobifida fusca Cellulases with Different Modes of Action

scientific article published on 05 March 2019

When substrate inhibits and inhibitor activates: implications of β-glucosidases

artículo científico publicado en 2017

Yeast mitochondrial DNA polymerase is a highly processive single-subunit enzyme.

artículo científico publicado en 2010

Lista de obras de

A pyranose dehydrogenase-based biosensor for kinetic analysis of enzymatic hydrolysis of cellulose by cellulases

Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I

Anomeric Selectivity and Product Profile of a Processive Cellulase

Endo-exo synergism in cellulose hydrolysis revisited.

Enzyme processivity changes with the extent of recalcitrant polysaccharide degradation

Human Chitotriosidase Is an Endo-Processive Enzyme

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.

Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

Kinetic insights into the role of the reductant in H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase

Kinetics of H2O2-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase

Measuring processivity

Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis

Mechanism of substrate inhibition in cellulose synergistic degradation

Multi-mode binding of Cellobiohydrolase Cel7A from Trichoderma reesei to cellulose

Processivity of cellobiohydrolases is limited by the substrate.

Selecting β-glucosidases to support cellulases in cellulose saccharification.

Strong cellulase inhibitors from the hydrothermal pretreatment of wheat straw

Surface character of pulp fibres studied using endoglucanases

The dissociation mechanism of processive cellulases

The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface − erosion model ⬇️

The liquid fraction from hydrothermal pretreatment of wheat straw provides lytic polysaccharide monooxygenases with both electrons and H2O2 co-substrate

Thermodynamic Relationships with Processivity in Serratia marcescens Family 18 Chitinases.

Thermodynamic Signatures of Substrate Binding for Three Thermobifida fusca Cellulases with Different Modes of Action

When substrate inhibits and inhibitor activates: implications of β-glucosidases

Yeast mitochondrial DNA polymerase is a highly processive single-subunit enzyme.