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

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 May 29;19(6):1600. doi: 10.3390/ijms19061600.
Hui-Bo Song 1 2,  Meng He 3,  Zhi-Peng Cai 4,  Kun Huang 5,  Sabine L Flitsch 6,  Li Liu 7,  Josef Voglmeir 8
Affiliations

Affiliations

  • 1 Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. 2013208001@njau.edu.cn.
  • 2 Department of Food Science, Zhejiang Pharmaceutical College, Ningbo 315100, China. 2013208001@njau.edu.cn.
  • 3 Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. 2015108040@njau.edu.cn.
  • 4 Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. caizhipeng@njau.edu.cn.
  • 5 Manchester Institute of Biotechnology, University of Manchester, Manchester M1 7DN, UK. kun.huang-3@manchester.ac.uk.
  • 6 Manchester Institute of Biotechnology, University of Manchester, Manchester M1 7DN, UK. sabine.flitsch@manchester.ac.uk.
  • 7 Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. lichen.liu@njau.edu.cn.
  • 8 Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. josef.voglmeir@njau.edu.cn.
PMID: 29844279 DOI: 10.3390/ijms19061600
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.

Keywords

Magallana gigas; UDP-galactose; UDP-glucose 4-epimerase; oyster metabolism.

Figures
Products