Immobilization of UDP-Galactose 4-Epimerase fromEscherichia colion the Yeast Cell Surface
| Autor: | Gang-Liang Huang, Qing-Sheng Qi, Jin-Yan Bi, Min Xiao, Peng George Wang, Chang Chen, Hou-Cheng Zhang |
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| Rok vydání: | 2006 |
| Předmět: |
DNA
Bacterial Uridine Diphosphate Glucose Saccharomyces cerevisiae medicine.disease_cause Polymerase Chain Reaction Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Uridine Diphosphate Galactose UDPglucose 4-Epimerase chemistry.chemical_compound Plasmid Escherichia coli medicine Cloning Molecular Molecular Biology chemistry.chemical_classification biology Organic Chemistry Electrophoresis Capillary General Medicine Enzymes Immobilized biology.organism_classification Enterobacteriaceae Enzyme assay Yeast carbohydrates (lipids) Enzyme chemistry Galactose biology.protein Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 70:2303-2306 |
| ISSN: | 1347-6947 0916-8451 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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