Mixed Aromatic Acyloin Condensations with Recombinant Benzaldehyde Lyase: Synthesis of α-Hydroxydihydrochalcones and Related α-Hydroxy Ketones

Recombinant benzaldehyde lyase (BAL), expressed and purified from E. coli strain JM‐109, was used to catalyze the condensation of a series of methoxybenzaldehydes and phenylacetaldehyde in the synthesis of α‐(R)‐hydroxydihydrochalcones. Enantiomerically pure 1‐hydroxy‐1,3‐diphenylpropan‐2‐ones and o...

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Bibliographic Details
Published in:Advanced synthesis & catalysis 2003-06, Vol.345 (6-7), p.819-824
Main Authors: Sanchez-Gonzalez, Monica, Rosazza, John P. N.
Format: Article
Language:English
Subjects:
acyloin condensation
benzaldehyde lyase
chemoenzymatic synthesis
flavonoid
α-hydroxydihydrochalcone
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Summary:Recombinant benzaldehyde lyase (BAL), expressed and purified from E. coli strain JM‐109, was used to catalyze the condensation of a series of methoxybenzaldehydes and phenylacetaldehyde in the synthesis of α‐(R)‐hydroxydihydrochalcones. Enantiomerically pure 1‐hydroxy‐1,3‐diphenylpropan‐2‐ones and o‐anisoin were also obtained as products of the BAL reaction. The R absolute configurations of chiral centers were determined by CD spectroscopy. α‐(R)‐Hydroxydihydrochalcones and 1‐hydroxy‐1,3‐diphenylpropan‐2‐ones are valuable synthons for chemoenzymatic syntheses of flavonoids. This is the first synthesis of α‐(R)‐hydroxydihydrochalcones by a microbial enzyme.
ISSN:1615-4150
1615-4169
DOI:10.1002/adsc.200303033