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Current Green Chemistry

Editor-in-Chief

ISSN (Print): 2213-3461
ISSN (Online): 2213-347X

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

Author(s): Alba Diaz-Rodriguez, Ivan Lavandera and Vicente Gotor

Volume 2 , Issue 2 , 2015

Page: [192 - 211] Pages: 20

DOI: 10.2174/2213346102666150120221227

Price: $65

Abstract

In recent years the usefulness of enzymatic systems to obtain a single stereoisomerically pure compound starting from a racemate has been expanded. Moreover, current advances in protein engineering, molecular biology and modeling tools are the basis to improve the catalytic properties of enzymes to face novel synthetic challenges. Also, medium engineering and novel immobilization methods of (bio)catalysts are enhancing the productivity of biocatalytic processes making them suitable for being scalable. The development of multienzymatic protocols and the combination of enzymes with other catalysts are providing a wide range of synthetic possibilities that are expanding the scope of these transformations even at industrial scale. Herein we will describe an overview of recent (chemo)enzymatic deracemizations, focusing on the strategy employed (dynamic kinetic resolution, stereoinversion, cyclic deracemization or enantioconvergent process), the type of substrate (e.g., alcohols, amines, carboxylic acid derivatives or carbonylic compounds), and the biocatalyst(s) used.

Keywords: Biocatalysis, cyclic deracemization, deracemization, dynamic kinetic resolution, enantioconvergent process, enzymes, organic synthesis, stereoinversion.

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