Non-chromatographic purification of thermostable endoglucanase from Thermotoga maritima by fusion with a hydrophobic elastin-like polypeptide.
Elastin-like polypeptide
Endoglucanase
Fusion expression
Inverse transition cycling
Thermostability
Journal
Protein expression and purification
ISSN: 1096-0279
Titre abrégé: Protein Expr Purif
Pays: United States
ID NLM: 9101496
Informations de publication
Date de publication:
09 2020
09 2020
Historique:
received:
22
10
2019
revised:
26
02
2020
accepted:
31
03
2020
pubmed:
24
4
2020
medline:
22
1
2021
entrez:
24
4
2020
Statut:
ppublish
Résumé
Endoglucanase EG12B from Thermotoga maritima is a thermophilic cellulase that has great potential for industrial applications. Here, to enable the selective purification of EG12B in a simple and efficient manner, an elastin-like polypeptide (ELP), which acts as a thermally responsive polypeptide, was fused with EG12B to enable its inverse phase transition cycling (ITC). A small gene library comprising ELPs from ELP
Identifiants
pubmed: 32325232
pii: S1046-5928(19)30567-4
doi: 10.1016/j.pep.2020.105634
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Recombinant Fusion Proteins
0
Elastin
9007-58-3
Cellulase
EC 3.2.1.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
105634Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.