Works by Väljamäe, Priit

Results: 14

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

Published in:

Biotechnology for Biofuels, 2019, v. 12, n. 1, p. N.PAG, doi. 10.1186/s13068-019-1578-5

By:

Kont, Riin;
Pihlajaniemi, Ville;
Borisova, Anna S.;
Aro, Nina;
Marjamaa, Kaisa;
Loogen, Judith;
Büchs, Jochen;
Eijsink, Vincent G. H.;
Kruus, Kristiina;
Väljamäe, Priit

Publication type:

Article

Enzyme kinetics by GH7 cellobiohydrolases on chromogenic substrates is dictated by non‐productive binding: insights from crystal structures and MD simulation.

Published in:

FEBS Journal, 2023, v. 290, n. 2, p. 379, doi. 10.1111/febs.16602

By:

Haataja, Topi;
Gado, Japheth E.;
Nutt, Anu;
Anderson, Nolan T.;
Nilsson, Mikael;
Momeni, Majid Haddad;
Isaksson, Roland;
Väljamäe, Priit;
Johansson, Gunnar;
Payne, Christina M.;
Ståhlberg, Jerry

Publication type:

Article

Human Chitotriosidase Is an Endo-Processive Enzyme.

Published in:

PLoS ONE, 2017, v. 12, n. 1, p. 1, doi. 10.1371/journal.pone.0171042

By:

Kuusk, Silja;
Sørlie, Morten;
Väljamäe, Priit

Publication type:

Article

Reducing end-specific fluorescence labeled celluloses for cellulase mode of action.

Published in:

Cellulose, 2010, v. 17, n. 1, p. 125, doi. 10.1007/s10570-009-9356-3

By:

Velleste, Riin;
Teugjas, Hele;
Väljamäe, Priit

Publication type:

Article

Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis.

Published in:

Biotechnology & Bioengineering, 2010, v. 106, n. 6, p. 871, doi. 10.1002/bit.22779

By:

Jalak, Jürgen;
Väljamäe, Priit

Publication type:

Article

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

Published in:

Biotechnology & Bioengineering, 2004, v. 86, n. 5, p. 503, doi. 10.1002/bit.10838

By:

Gruno, Marju;
Väljamäe, Priit;
Pettersson, Göran;
Johansson, Gunnar

Publication type:

Article

Synergistic cellulose hydrolysis can be described in terms of fractal-like kinetics.

Published in:

Biotechnology & Bioengineering, 2003, v. 84, n. 2, p. 254

By:

Priit Väljamäe;
Kalle Kipper;
Göran Pettersson;
Gunnar Johansson

Publication type:

Article

Enzyme processivity changes with the extent of recalcitrant polysaccharide degradation.

Published in:

FEBS Letters, 2014, v. 588, n. 24, p. 4620, doi. 10.1016/j.febslet.2014.10.034

By:

Hamre, Anne Grethe;
Lorentzen, Silje Benedicte;
Väljamäe, Priit;
Sørlie, Morten

Publication type:

Article

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

Published in:

Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-19561-8

By:

Kont, Riin;
Bissaro, Bastien;
Eijsink, Vincent G. H.;
Väljamäe, Priit

Publication type:

Article

Multi-Mode Binding of Cellobiohydrolase Cel7A from Trichoderma reesei to Cellulose.

Published in:

PLoS ONE, 2014, v. 9, n. 9, p. 1, doi. 10.1371/journal.pone.0108181

By:

Jalak, Jürgen;
Väljamäe, Priit

Publication type:

Article

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

Published in:

Biotechnology for Biofuels, 2017, v. 10, p. 1, doi. 10.1186/s13068-016-0690-z

By:

Kuusk, Silja;
Väljamäe, Priit

Publication type:

Article

Strong cellulase inhibitors from the hydrothermal pretreatment of wheat straw.

Published in:

Biotechnology for Biofuels, 2013, v. 6, n. 1, p. 1, doi. 10.1186/1754-6834-6-135

By:

Kont, Riin;
Kurašin, Mihhail;
Teugjas, Hele;
Väljamäe, Priit

Publication type:

Article

Selecting β-glucosidases to support cellulases in cellulose saccharification.

Published in:

Biotechnology for Biofuels, 2013, v. 6, n. 1, p. 1, doi. 10.1186/1754-6834-6-105

By:

Teugjas, Hele;
Väljamäe, Priit

Publication type:

Article

Product inhibition of cellulases studied with 14C-labeled cellulose substrates.

Published in:

Biotechnology for Biofuels, 2013, v. 6, n. 1, p. 1, doi. 10.1186/1754-6834-6-104

By:

Teugjas, Hele;
Väljamäe, Priit

Publication type:

Article

Works by Väljamäe, Priit

The liquid fraction from hydrothermal pretreatment of wheat straw provides lytic polysaccharide monooxygenases with both electrons and H<sub>2</sub>O<sub>2</sub> co-substrate.

Enzyme kinetics by GH7 cellobiohydrolases on chromogenic substrates is dictated by non‐productive binding: insights from crystal structures and MD simulation.

Human Chitotriosidase Is an Endo-Processive Enzyme.

Reducing end-specific fluorescence labeled celluloses for cellulase mode of action.

Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis.

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

Synergistic cellulose hydrolysis can be described in terms of fractal-like kinetics.

Enzyme processivity changes with the extent of recalcitrant polysaccharide degradation.

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

Multi-Mode Binding of Cellobiohydrolase Cel7A from Trichoderma reesei to Cellulose.

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

Strong cellulase inhibitors from the hydrothermal pretreatment of wheat straw.

Selecting β-glucosidases to support cellulases in cellulose saccharification.

Product inhibition of cellulases studied with <sup>14</sup>C-labeled cellulose substrates.