Characterization of a recombinant D-mannose-producing D-lyxose isomerase from Caldanaerobius polysaccharolyticus.
Aldose-Ketose Isomerases
/ chemistry
Amino Acid Sequence
Bacterial Proteins
/ chemistry
Escherichia coli
/ genetics
Firmicutes
/ enzymology
Fructose
/ metabolism
Hot Temperature
Hydrogen-Ion Concentration
Kinetics
Manganese
Mannose
/ biosynthesis
Protein Multimerization
Recombinant Proteins
/ chemistry
Substrate Specificity
Caldanaerobius polysaccharolyticus
d-fructose
d-lyxose isomerase
d-mannose
Journal
Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761
Informations de publication
Date de publication:
Aug 2020
Aug 2020
Historique:
received:
24
12
2019
revised:
07
03
2020
accepted:
10
03
2020
entrez:
13
6
2020
pubmed:
13
6
2020
medline:
16
1
2021
Statut:
ppublish
Résumé
Recently, functional sugars, such as d-mannose, have attracted considerable attention due to their excellent physiological benefits for human health and wide applications in food and pharmaceutical industries. Therefore, d-mannose production using a sugar isomerase such as d-lyxose isomerase (d-LIase) has emerged as a research hotspot owing to its advantages over plant extraction and chemical synthesis methods. In this study, a putative d-LIase gene from Caldanaerobius polysaccharolyticus was cloned and expressed in Escherichia coli. Then, a biochemical characterization of the recombinant d-LIase was carried out and its potential use in d-mannose production also assessed. Results showed that d-LIase exhibited its maximum activity under these optimal conditions: temperature of 65 °C, a pH of 6.5, and the Mn
Identifiants
pubmed: 32527523
pii: S0141-0229(20)30046-6
doi: 10.1016/j.enzmictec.2020.109553
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Recombinant Proteins
0
Fructose
30237-26-4
Manganese
42Z2K6ZL8P
Aldose-Ketose Isomerases
EC 5.3.1.-
D-lyxose ketol-isomerase
EC 5.3.1.15
Mannose
PHA4727WTP
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
109553Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors also declared no conflict of interest.