A unique self-truncation of bacterial GH5 endoglucanases leads to enhanced activity and thermostability
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1741-7007
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
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
- Urheber
-
Wu, Mei-Huey
Kao, Mu-Rong
Li, Chen-Wei
Yu, Su-May
Ho, Tuan-Hua David
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1186/s12915-022-01334-y
- URN
-
urn:nbn:de:101:1-2022080609224270926804
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:33 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Wu, Mei-Huey
- Kao, Mu-Rong
- Li, Chen-Wei
- Yu, Su-May
- Ho, Tuan-Hua David
- SpringerLink (Online service)
Ähnliche Objekte (12)
Thermostability of enzymes
Fiberwise homology truncation
Fiberwise Homology Truncation
Thermostability in endoglucanases is fold-specific
Consistent mutational paths predict eukaryotic thermostability
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
Unique lipid composition maintained by extracellular blockade leads to prooncogenicity
Thermostability of enzymes
Fiberwise homology truncation
Fiberwise Homology Truncation
Thermostability in endoglucanases is fold-specific
Consistent mutational paths predict eukaryotic thermostability
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
Unique lipid composition maintained by extracellular blockade leads to prooncogenicity
Thermostability of enzymes
Fiberwise homology truncation
Fiberwise Homology Truncation
Thermostability in endoglucanases is fold-specific
Consistent mutational paths predict eukaryotic thermostability
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