A unique self-truncation of bacterial GH5 endoglucanases leads to enhanced activity and thermostability
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1741-7007
- 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 unique self-truncation of bacterial GH5 endoglucanases leads to enhanced activity and thermostability ; volume:20 ; number:1 ; day:9 ; month:6 ; year:2022 ; pages:1-18 ; date:12.2022
BMC biology ; 20, Heft 1 (9.6.2022), 1-18, 12.2022
- Creator
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Wu, Mei-Huey
Kao, Mu-Rong
Li, Chen-Wei
Yu, Su-May
Ho, Tuan-Hua David
- Contributor
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SpringerLink (Online service)
- DOI
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10.1186/s12915-022-01334-y
- URN
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urn:nbn:de:101:1-2022080609224270926804
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:33 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
- Wu, Mei-Huey
- Kao, Mu-Rong
- Li, Chen-Wei
- Yu, Su-May
- Ho, Tuan-Hua David
- SpringerLink (Online service)
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Unique lipid composition maintained by extracellular blockade leads to prooncogenicity
Thermostability of enzymes
Fiberwise homology truncation
Fiberwise Homology Truncation
Consistent mutational paths predict eukaryotic thermostability
Thermostability in endoglucanases is fold-specific
Cellulase protein engineering towards improved thermostability
Unique N-glycosylation of a recombinant exo-inulinase from Kluyveromyces cicerisporus and its effect on enzymatic activity and thermostability
Optimal Truncation in Matching Markets
Hamiltonian Truncation with larger dimensions
Endoglucanases: insights into thermostability for biofuel applications
Improving the thermostability and stress tolerance of an archaeon hyperthermophilic superoxide dismutase by fusion with a unique N-terminal domain