Abstract
A UDP-glycosyltransferase from Bacillus licheniformis was exploited for the glycosylation of phloretin. The in vitro glycosylation reaction confirmed the production of five phloretin glucosides, including three novel glucosides. Consequently, we demonstrated the application of the same glycosyltransferase for the efficient whole-cell biocatalysis of phloretin in engineered Escherichia coli.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacillus / enzymology*
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Chromatography, High Pressure Liquid
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Escherichia coli
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Escherichia coli Proteins / metabolism*
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Genetic Engineering
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Glycosylation
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Glycosyltransferases / metabolism*
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Magnetic Resonance Spectroscopy
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Molecular Structure
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Phloretin / metabolism*
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Tandem Mass Spectrometry
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Uridine Diphosphate Sugars / metabolism
Substances
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Escherichia coli Proteins
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Uridine Diphosphate Sugars
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YjiC protein, E coli
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Glycosyltransferases
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Phloretin