Characterization of a novel sucrose phosphorylase from Paenibacillus elgii and its use in biosynthesis of α-arbutin.
Molecular chaperone
Paenibacillus elgii
Sucrose phosphorylase
α-arbutin
Journal
World journal of microbiology & biotechnology
ISSN: 1573-0972
Titre abrégé: World J Microbiol Biotechnol
Pays: Germany
ID NLM: 9012472
Informations de publication
Date de publication:
07 Dec 2023
07 Dec 2023
Historique:
received:
14
09
2023
accepted:
22
11
2023
medline:
11
12
2023
pubmed:
7
12
2023
entrez:
6
12
2023
Statut:
epublish
Résumé
α-Arbutin, a naturally occurring glycosylated derivative of hydroquinone (HQ), effectively inhibits melanin biosynthesis in epidermal cells. It is widely recognized as a fourth-generation whitening agent within the cosmetic industry. Currently, enzymatic catalysis is universally deemed the safest and most efficient method for α-arbutin synthesis. Sucrose phosphorylase (SPase), one of the most frequently employed glycosyltransferases, has been extensively reported for α-arbutin synthesis. In this study, a previously reported SPase known for its effectiveness in synthesizing α-arbutin, was used as a probe sequence to identify a novel SPase from Paenibacillus elgii (PeSP) in the protein database. The sequence similarity between PeSP and the probe was 39.71%, indicating a degree of novelty. Subsequently, the gene encoding PeSP was coexpressed with the molecular chaperone pG-Tf2 in Escherichia coli, significantly improving PeSP's solubility. Following this, PeSP was characterized and employed for α-arbutin biosynthesis. The specific activity of co-expressed PeSP reached 169.72 U/mg, exhibited optimal activity at 35℃ and pH 7.0, with a half-life of 3.6 h under the condition of 35℃. PeSP demonstrated excellent stability at pH 6.5-8.5 and sensitivity to high concentrations of metal ions. The kinetic parameters K
Identifiants
pubmed: 38057640
doi: 10.1007/s11274-023-03853-4
pii: 10.1007/s11274-023-03853-4
doi:
Substances chimiques
sucrose phosphorylase
EC 2.4.1.7
hydroquinone
XV74C1N1AE
Hydroquinones
0
Arbutin
C5INA23HXF
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
24Subventions
Organisme : National Natural Science Foundation of China
ID : Nos. 31972464
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer Nature B.V.
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