UDP-Glucose 4-Epimerase and β-1,4-Galactosyltransferase from the Oyster Magallana gigas as Valuable Biocatalysts for the Production of Galactosylated Products

Uridine diphosphate galactose (UDP-galactose) is a valuable building block in the enzymatic synthesis of galactose-containing glycoconjugates. UDP-glucose 4-epimerase (UGE) is an enzyme which catalyzes the reversible conversion of abundantly available UDP-glucose to UDP-galactose. Herein, we describ...

Full description

Saved in:
Bibliographic Details
Published in:International journal of molecular sciences 2018-05, Vol.19 (6), p.1600
Main Authors: Song, Hui-Bo, He, Meng, Cai, Zhi-Peng, Huang, Kun, Flitsch, Sabine L, Liu, Li, Voglmeir, Josef
Format: Article
Language:English
Subjects:
Biocatalysts
Cloning
Enzymatic activity
Enzymatic synthesis
Epimerase
Galactose
Glucose
Glycoconjugates
High performance liquid chromatography
Ions
Magallana gigas
Mass spectrometry
Mass spectroscopy
Metal ions
Nitrophenol
oyster metabolism
Photometry
Purification
Thermal stability
UDP-galactose
UDP-glucose 4-epimerase
Uridine
Xylose
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Uridine diphosphate galactose (UDP-galactose) is a valuable building block in the enzymatic synthesis of galactose-containing glycoconjugates. UDP-glucose 4-epimerase (UGE) is an enzyme which catalyzes the reversible conversion of abundantly available UDP-glucose to UDP-galactose. Herein, we described the cloning, expression, purification, and biochemical characterization of an unstudied UGE from the oyster (MgUGE). Activity tests of recombinantly expressed MgUGE, using HPLC (high-performance liquid chromatography), mass spectrometry, and photometric assays, showed an optimal temperature of 16 °C, and reasonable thermal stability up to 37 °C. No metal ions were required for enzymatic activity. The simple nickel-affinity-purification procedure makes MgUGE a valuable biocatalyst for the synthesis of UDP-galactose from UDP-glucose. The biosynthetic potential of MgUGE was further exemplified in a coupled enzymatic reaction with an oyster-derived β-1,4-galactosyltransferase (MgGalT7), allowing the galactosylation of the model substrate -nitrophenol xylose ( NP-xylose) using UDP-glucose as the starting material.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms19061600