Heterologous expression of Deinococcus geothermalis amylosucrase in Corynebacterium glutamicum for luteolin glucoside production.
Amylosucrases
Corynebacterium glutamicum
Deinococcus geothermalis
Heterologous expression
Luteolin
Transglucosylation
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:
Apr 2020
Apr 2020
Historique:
received:
23
09
2019
revised:
12
12
2019
accepted:
26
12
2019
entrez:
10
3
2020
pubmed:
10
3
2020
medline:
2
10
2020
Statut:
ppublish
Résumé
Amylosucrase (ASase) has great industrial potential owing to its multifunctional activities, including transglucosylation, polymerization, and isomerization. In the present study, the properties of Deinococcus geothermalis ASase (DGAS) expressed in Corynebacterium glutamicum (cDGAS) and purified via Ni-NTA affinity chromatography were compared to those of DGAS expressed in Escherichia coli (eDGAS). The pH profile of cDGAS was similar to that of eDGAS, whereas the temperature profile of cDGAS was lower than that of eDGAS. The melting temperature of both enzymes did not differ significantly. Interestingly, polymerization activity was slightly lower in cDGAS than in eDGAS, whereas luteolin (an acceptor molecule) transglucosylation activity in cDGAS was 10 % higher than that in eDGAS. Analysis of protein secondary structure via circular dichroism spectroscopy revealed that cDGAS had a lower strand/helix ratio than eDGAS. The present results indicate that cDGAS is of greater industrial significance than eDGAS.
Identifiants
pubmed: 32146930
pii: S0141-0229(19)30243-1
doi: 10.1016/j.enzmictec.2019.109505
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Glucosides
0
Glucosyltransferases
EC 2.4.1.-
amylosucrase
EC 2.4.1.4
Luteolin
KUX1ZNC9J2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
109505Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.