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Updated: Jul 20, 2026
Mating-based Overexpression Library Screening in Yeast
Published on: July 6, 2018
Immobilization of UDP-galactose 4-epimerase from Escherichia coli on the yeast cell surface
Hou-Cheng Zhang1, Jin-Yan Bi, Chang Chen
1The State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China. zhanghoucheng@sdu.edu.cn
Abstract:
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 cerevisiae 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.
