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Int. J. Mol. Sci. 2018, 19(6), 1600; https://doi.org/10.3390/ijms19061600

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

1
Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
2
Department of Food Science, Zhejiang Pharmaceutical College, Ningbo 315100, China
3
Manchester Institute of Biotechnology, University of Manchester, Manchester M1 7DN, UK
*
Authors to whom correspondence should be addressed.
Received: 30 April 2018 / Revised: 23 May 2018 / Accepted: 24 May 2018 / Published: 29 May 2018
(This article belongs to the Special Issue Molecular Transformations of Natural Products)
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Abstract

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 Magallana gigas (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 para-nitrophenol xylose (pNP-xylose) using UDP-glucose as the starting material. View Full-Text
Keywords: UDP-galactose; UDP-glucose 4-epimerase; Magallana gigas; oyster metabolism UDP-galactose; UDP-glucose 4-epimerase; Magallana gigas; oyster metabolism
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Song, H.-B.; He, M.; Cai, Z.-P.; Huang, K.; Flitsch, S.L.; Liu, L.; Voglmeir, J. UDP-Glucose 4-Epimerase and β-1,4-Galactosyltransferase from the Oyster Magallana gigas as Valuable Biocatalysts for the Production of Galactosylated Products. Int. J. Mol. Sci. 2018, 19, 1600.

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