Enantiospecific Production of S-(-)-2-Hydroxypropiophenone Mediated by Benzoylformate Decarboxylase from Acinetobacter Calcoaceticus |
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| Authors: | Elizabeth Prosen Owen P. Ward Scott Collins Nolan J. Dewdney Yaping Hong Richard Wilcocks |
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| Affiliation: | a Departments of Biology, University of Waterloo, Waterloo, Ontario, Canadab Departments of Chemistry, University of Waterloo, Waterloo, Ontario, Canada |
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| Abstract: | Whole cells of Acinetobacter calcoaceticus, grown in a medium containing mandelate, converted benzoylformate and acetaldehyde into the acyloin compound 2-hydroxypropiophenone. The optical purity of the product was found to be greater than 98%. The absolute configuration of the biotransformation product at the carbinol carbon was found to be (S). The enzyme responsible for this bioconversion was confirmed as benzoylformate decarboxylase by the demonstration that the purified homogeneous enzyme catalysed the condensation reaction. |
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| Keywords: | Acinetobacter calcoaceticus 2-hydroxypropiophenone acyloin benzoylformate decarboxylase biotransformation |
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