Immobilization of UDP-Galactose 4-Epimerase from Escherichia coli on the Yeast Cell Surface

Hou-Cheng ZHANG; Jin-Yan BI; Chang CHEN; Gang-Liang HUANG; Qing-Sheng QI; Min XIAO; Peng George WANG

doi:10.1271/bbb.60134

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Immobilization of UDP-Galactose 4-Epimerase from Escherichia coli on the Yeast Cell Surface

Hou-Cheng ZHANG, Jin-Yan BI, Chang CHEN, Gang-Liang HUANG, Qing-Sheng QI, Min XIAO, Peng George WANG

著者情報

キーワード: UDP-galactose 4-epimerase, Saccharomyces cereviae, cell surface

ジャーナルフリー早期公開

論文ID: 60134

DOI https://doi.org/10.1271/bbb.60134

この記事には本公開記事があります。

The final version of this article is now available: Vol. 70 (2006) , No. 9 p.2303

詳細

抄録

UDP-galactose 4-epimerase (EC 5.1.3.2, Gal E) from Escherichia coli catalyzes the reversible reaction between UDP-galactose and UDP-glucose. In this study, the Gal E gene from E. coli, coding UDP-galactose 4-epimerase, was cloned into pYD1 plasmid and then transformed into Saccharomyces cereviae EBY100 for expression of Gal E on the cell surface. Enzyme activity analyses with EBY100 cells showed that the enzyme displayed on the yeast cell surface was very active in the conversion between UDP-Glc and UDP-Gal. It took about 3 min to reach equilibrium from UDP-galactose to UDP-glucose.

責任著者(Corresponding author)

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