Tuning the pH profile of β-glucuronidase by rational site-directed mutagenesis for efficient transformation of glycyrrhizin.
Arginine
Rational design
pH shift
pH stability
β-Glucuronidase
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
Jun 2019
Jun 2019
Historique:
received:
21
12
2018
accepted:
20
03
2019
revised:
16
03
2019
pubmed:
6
5
2019
medline:
13
9
2019
entrez:
6
5
2019
Statut:
ppublish
Résumé
In this study, we aimed to shift the optimal pH of acidic β-glucuronidase from Aspergillus oryzae Li-3 (PGUS) to the neutral region by site-directed mutagenesis, thus allowing high efficient biotransformation of glycyrrhizin (GL) into glycyrrhetinic acid (GA) under higher pH where the solubility of GL could be greatly enhanced. Based on PGUS structure analysis, five critical aspartic acid and glutamic acid residues were replaced with arginine on the surface to generate a variant 5Rs with optimal pH shifting from 4.5 to 6.5. The catalytic efficiency (k
Identifiants
pubmed: 31055652
doi: 10.1007/s00253-019-09790-3
pii: 10.1007/s00253-019-09790-3
doi:
Substances chimiques
Aspartic Acid
30KYC7MIAI
Glutamic Acid
3KX376GY7L
Glycyrrhizic Acid
6FO62043WK
Glucuronidase
EC 3.2.1.31
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
4813-4823Subventions
Organisme : National Natural Science Foundation of China
ID : 21425624,
Organisme : National Natural Science Foundation of China
ID : 21736002
Organisme : National Natural Science Foundation of China
ID : 21878021
Organisme : Beijing Institute of Technology Research Fund Program for Young Scholars
ID : None