Edward R. Biehl
Southern Methodist University
304 Papers
1.7K Citations
Edward R. Biehl is an academic researcher from Southern Methodist University. The author has contributed to research in topics: Aryne & Crystal structure. The author has an hindex of 27, co-authored 304 publications. Previous affiliations of Edward R. Biehl include Mansoura University & Food and Drug Administration.
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Papers
Nitrilase-catalyzed selective hydrolysis of dinitriles and green access to the cyanocarboxylic acids of pharmaceutical importance
TL;DR: It has been found that nitrilase bll6402 effectively hydrolyzed α,ω-dinitriles to ω-cyanocarboxylic acids, and the selectivity was independent of the substrate chain length.
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Enantioselective Reduction of Diaryl Ketones Catalyzed by a Carbonyl Reductase from Sporobolomyces salmonicolor and its Mutant Enzymes
TL;DR: The present study provides valuable information about the catalytic properties of the carbonyl reductase SSCR toward the reduction of diaryl ketones, serving as basis for further engineering of this enzyme to develop efficient biocatalysts for highly enantiospecific reduction of daily ketones without high electronic dissymmetry or an ortho-substituent on one of the aryl groups.
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Asymmetric Synthesis of Both Antipodes of β-Hydroxy Nitriles and β-Hydroxy Carboxylic Acids via Enzymatic Reduction or Sequential Reduction/Hydrolysis
TL;DR: Use of isolated carbonyl reductases in the reduction of aromatic beta-ketonitriles have completely eliminated the competing alpha-ethylation, which is often observed with whole cell biocatalysts, and allows ready access to both antipodes of chiral beta-Hydroxy nitriles and beta-hydroxy carboxylic acids of pharmaceutical importance with excellent optical purity.
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Asymmetric reduction of beta-ketonitriles with a recombinant carbonyl reductase and enzymatic transformation to optically pure beta-hydroxy carboxylic acids.
TL;DR: (R)-β-Hydroxy nitriles were obtained via a reduction catalyzed by a recombinant carbonyl reductase with excellent optical purity and were further converted to (R)- β-hydroxy carboxylic acids via a nitrilase-catalyzed hydrolysis.
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