Cloning, expression and characterization of a thermo-alkali-stable xylanase from Aspergillus oryzae LC1 in Escherichia coli BL21(DE3).
Alkalies
/ chemistry
Amino Acid Sequence
Aspergillus oryzae
/ chemistry
Chromatography, Ion Exchange
Cloning, Molecular
Endo-1,4-beta Xylanases
/ genetics
Enzyme Stability
Escherichia coli
/ genetics
Fungal Proteins
/ genetics
Gene Expression
Genetic Vectors
/ chemistry
Hydrogen-Ion Concentration
Molecular Weight
Recombinant Proteins
/ genetics
Sequence Alignment
Sequence Homology, Amino Acid
Temperature
Xylans
/ chemistry
Aspergillus oryzae
Gene cloning
Overexpression
Thermo-alkali-stable xylanase
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:
04 2020
04 2020
Historique:
received:
07
06
2019
revised:
26
09
2019
accepted:
11
12
2019
pubmed:
16
12
2019
medline:
8
1
2021
entrez:
16
12
2019
Statut:
ppublish
Résumé
In the present investigation, cloning and overexpression of xylanase (XynF1), the main xylanase of A. oryzae LC1, was performed in prokaryotic system E. coli BL21(DE3) to produce recombinant xylanase with high titer of specific activity (1037.3 U/mg), which was 9.3-fold higher than the native strain. Further, the recombinant XynF1 of size 37 kDa was purified using Ni
Identifiants
pubmed: 31838156
pii: S1046-5928(19)30295-5
doi: 10.1016/j.pep.2019.105551
pii:
doi:
Substances chimiques
Alkalies
0
Fungal Proteins
0
Recombinant Proteins
0
Xylans
0
Endo-1,4-beta Xylanases
EC 3.2.1.8
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
105551Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no conflict of interest.