Lipase enantiopure compound biocatalytic

P. Berglund, K. Hull, Biocatalytic Synthesis of Enantiopure Compounds Using Lipases, in R. N. Patel (Ed.), Stereoselective Biocatalysis, Marcel Dekker, New York, Basel, 2000, pp. 633-657. 

Biocatalytic Synthesis of Enantiopure Compounds Using Lipases... 

Lipases are of remarkable practical interest since they have been used in numerous biocatalytic applications, such as kinetic resolution of alcohols and carboxyl esters (both in water and in non-aqueous media) [1], regioselective acylations of poly-hydroxylated compounds, and the preparation of enantiopure amino acids and amides [2, 3]. Moreover, lipases are stable in organic solvents, do not require cofactors, possess broad substrate specificity, and exhibit, in general, a high enantioselectivity. All these features have contributed to make hpases the class of enzyme with the highest number of biocatalytic applications carried out in neat organic solvents. 

Clearly, most biocatalytic reactions for the production of fine chemicals are used to obtain enantiopure or enantioenriched compounds, and only a minor number of syntheses lead to products without chiral centers. More than 65 applications of immobilized enzymes or whole cells for industrial research and production have been treated in this review, and it can be stated that approximately 80% utilize the class of hydrolytic enzymes. This number reflects the ease of handling and the broad utility of these enzymes. The reported hydrolytic enzyme applications mainly involve lipases, whereas other hydrolases can only be found in fewer but nevertheless just as attractive cases. The broad field of asymmetric synthesis (e.g., asymmetric reduction/oxidation) is defi-... 

---