Immobilization of UDP-Galactose 4-Epimerase from Escherichia coli on the Yeast Cell Surface
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概要
- 論文の詳細を見る
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.
- 社団法人 日本農芸化学会の論文
- 2007-09-23
著者
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Huang Gang-liang
The State Key Laboratory Of Microbial Technology Shandong University
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Wang Peng
State Key Laboratory Of Microbial Technology (sklmt) Shandong University
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Bi Jin-yan
The State Key Laboratory Of Microbial Technology Shandong University
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ZHANG Hou-Cheng
The State Key Laboratory of Microbial Technology, Shandong University
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CHEN Chang
The State Key Laboratory of Microbial Technology, Shandong University
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QI Qing-Sheng
The State Key Laboratory of Microbial Technology, Shandong University
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XIAO Min
The State Key Laboratory of Microbial Technology, Shandong University
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WANG Peng
The State Key Laboratory of Microbial Technology, Shandong University
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Xiao Min
The State Key Laboratory Of Microbial Technology Shandong University
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Qi Qing-sheng
State Key Laboratory Of Microbial Technology (sklmt) Shandong University
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Zhang Hou-cheng
The State Key Laboratory Of Microbial Technology Shandong University
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Chen Chang
State Key Laboratory Of Microbial Technology (sklmt) Shandong University
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