Enhancement of the Isomerization Activity and Thermostability of Cellobiose 2-Epimerase from
catalytic direction
cellobiose 2-epimerase
flexible loop
isomerization activity
molecular dynamics simulation
thermostability
Journal
Journal of agricultural and food chemistry
ISSN: 1520-5118
Titre abrégé: J Agric Food Chem
Pays: United States
ID NLM: 0374755
Informations de publication
Date de publication:
17 Feb 2021
17 Feb 2021
Historique:
pubmed:
6
2
2021
medline:
15
5
2021
entrez:
5
2
2021
Statut:
ppublish
Résumé
Cellobiose 2-epimerase (CE) offers a promising enzymatic approach to produce lactulose. However, its application is limited by the unsatisfactory isomerization activity and thermostability. Our study attempted to optimize the catalytic performances of CEs by flexible loop exchange, for which four mutants were constructed using
Identifiants
pubmed: 33541071
doi: 10.1021/acs.jafc.0c07073
doi:
Substances chimiques
Cellobiose
16462-44-5
Lactulose
4618-18-2
Racemases and Epimerases
EC 5.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM