|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|69297||48738||2016||7 صفحه PDF||سفارش دهید||دانلود رایگان|
• Enzymatic reduction of racemic α-substituted ketones and simultaneous dynamic kinetic resolution.
• Stereoselective preparation of homochiral α-substituted chiral alcohols.
• Reductions of N-protected α-amino ketones provided N-protected α-amino alcohols in high de and ee.
• Choice of buffer is crucial for the reduction of an α-methyl ketone to the corresponding alcohol in high deand ee.
• Glucose dehydrogenase is acting as a ketoreductase.
Racemic α-substituted ketones were converted to the corresponding chiral alcohols with high diastereo- and enantioselectivities using enzymatic reduction with concomitant dynamic kinetic resolution. Reductions of N-protected α-amino ketones by microorganisms and commercial enzymes provided N-protected α-amino alcohols. Choice of buffer was found to be a crucial factor for the successful reduction and simultaneous dynamic resolution of an α-methyl ketone to the corresponding chiral alcohol.
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Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 133, November 2016, Pages 20–26