Expression, Folding, and Activation of Halophilic Alkaline Phosphatase in Non-Halophilic Brevibacillus choshinensis.
Activation
Alkaline phosphatase
Folding
Halomonas
Halophile
Journal
The protein journal
ISSN: 1875-8355
Titre abrégé: Protein J
Pays: Netherlands
ID NLM: 101212092
Informations de publication
Date de publication:
02 2020
02 2020
Historique:
pubmed:
18
11
2019
medline:
23
9
2020
entrez:
18
11
2019
Statut:
ppublish
Résumé
Halophilic enzymes contain a large number of acidic amino acids and marginal large hydrophobic amino acids, which make them highly soluble even under strongly hydrophobic conditions. This characteristic of halophilic enzymes provides potential for their industrial application. However, halophilic enzymes easily degrade when used for industrial applications compared with enzymes from other extremophiles because of their instability in low-salt environments. We aimed to clarify the stabilization mechanism of halophilic enzymes. We previously attempted to express halophilic alkaline phosphatase from Halomonas (HaALP) in non-halophilic E. coli. However, the expressed HaALP showed little activity. Therefore, we overexpressed HaALP in Gram-positive non-halophilic Brevibacillus choshinensis in this study, which was successfully expressed and purified in its active form. HaALP was denatured in 6 M urea, refolded using various salts and the non-ionic osmolyte trimethylamine N-oxide (TMAO), and assessed by native polyacrylamide gel electrophoresis. HaALP refolded in 3 M NaCl or 3 M TMAO containing Na
Identifiants
pubmed: 31734848
doi: 10.1007/s10930-019-09874-z
pii: 10.1007/s10930-019-09874-z
doi:
Substances chimiques
Methylamines
0
Sodium Chloride
451W47IQ8X
Alkaline Phosphatase
EC 3.1.3.1
trimethyloxamine
FLD0K1SJ1A
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
46-53Références
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