A simple enzymatic assay for the quantification of C1-specific cellulose oxidation by lytic polysaccharide monooxygenases
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1573-6776
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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A simple enzymatic assay for the quantification of C1-specific cellulose oxidation by lytic polysaccharide monooxygenases ; volume:42 ; number:1 ; day:20 ; month:11 ; year:2019 ; pages:93-102 ; date:1.2020
Biotechnology letters ; 42, Heft 1 (20.11.2019), 93-102, 1.2020
- Creator
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Keller, M. B.
Felby, C.
Labate, C. A.
Pellegrini, V. O. A.
Higasi, P.
Singh, R. K.
Polikarpov, I.
Blossom, B. M.
- Contributor
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SpringerLink (Online service)
- DOI
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10.1007/s10529-019-02760-9
- URN
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urn:nbn:de:101:1-2020041122072493137731
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:58 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Keller, M. B.
- Felby, C.
- Labate, C. A.
- Pellegrini, V. O. A.
- Higasi, P.
- Singh, R. K.
- Polikarpov, I.
- Blossom, B. M.
- SpringerLink (Online service)
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The yeast Geotrichum candidum encodes functional lytic polysaccharide monooxygenases
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Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases
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Lytic polysaccharide monooxygenases (LPMOs) facilitate cellulose nanofibrils production
On the functional characterization of lytic polysaccharide monooxygenases (LPMOs)
Four cellulose-active lytic polysaccharide monooxygenases from Cellulomonas species
The yeast Geotrichum candidum encodes functional lytic polysaccharide monooxygenases
Lytic polysaccharide monooxygenases from Myceliophthora thermophila C1 differ in substrate preference and reducing agent specificity
Evolution of substrate specificity in bacterial AA10 lytic polysaccharide monooxygenases
Enzymatic debranching is a key determinant of the xylan-degrading activity of family AA9 lytic polysaccharide monooxygenases
Functional characterization of fungal lytic polysaccharide monooxygenases for cellulose surface oxidation
Carboxylation of sulfated cellulose nanocrystals by family AA9 lytic polysaccharide monooxygenases
Transcriptional and secretome analysis of Rasamsonia emersonii lytic polysaccharide mono-oxygenases
Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases
Classification of fungal and bacterial lytic polysaccharide monooxygenases
Lytic polysaccharide monooxygenases (LPMOs) facilitate cellulose nanofibrils production
On the functional characterization of lytic polysaccharide monooxygenases (LPMOs)
Four cellulose-active lytic polysaccharide monooxygenases from Cellulomonas species
The yeast Geotrichum candidum encodes functional lytic polysaccharide monooxygenases
Lytic polysaccharide monooxygenases from Myceliophthora thermophila C1 differ in substrate preference and reducing agent specificity
Evolution of substrate specificity in bacterial AA10 lytic polysaccharide monooxygenases
Enzymatic debranching is a key determinant of the xylan-degrading activity of family AA9 lytic polysaccharide monooxygenases
Functional characterization of fungal lytic polysaccharide monooxygenases for cellulose surface oxidation
Carboxylation of sulfated cellulose nanocrystals by family AA9 lytic polysaccharide monooxygenases