Esterase Pseudomonas fluorescens lipase

Other similar lipase/esterase resolution processes have been developed such as the use of Bacillus that esterase to produce the substituted propanoic acids that are precursors of non-steroidal anti-inflammatory drags, snch as naproxen and ibuprofen etc., and the formation of chiral amines by Celgene. Other methods start from prochiral precursors and have the advantage that enantioselective synthesis allows the production of particular isomers in yields approaching 100%, rather than the 50% yields characteristic of resolution processes. For instance Hoechst have patented the production of enantiomers using Pseudomonas fluorescens lipase to either acylate diols or hydrolyse diacetate esters. 

The biocatalytic acetylation of prochiral bis(hydroxymethyl)phenylphosphine oxide 277 and the biocatalytic hydrolysis of prochiral bisfmethoxycarbonylmethyl) phenylphosphine oxide 279 was subjected to hydrolysis in a phosphate buffer in the presence of several hydrolases (PLE, PPL, AHS, Amano-AK, and Amano-PS), of which only porcine liver esterase (PLE) proved to be efficient. The best results were attained with Pseudomonas fluorescens lipase (PFL) in chloroform which allowed the compound 278 to be obtained in yields up to 76% and with ee up to 79%. Absolute configuration of the (5)-278 was determined by means of chemical correlation to the earlier described compound (/ )-282, as shown in Scheme 91 [185]. 

One of the reactions catalyzed by esterases and lipases is the reversible hydrolysis of esters (Figure 1 reaction 2). These enzymes also catalyze transesterifications and the asymmetrization of meso -substrates (Section 13.2.3.1.1). Many esterases and lipases are commercially available, making them easy to use for screening desired biotransformations without the need for culture collections and/or fermentation capabilities. As more and more research has been conducted with these enzymes, a less empirical approach is being taken due to the different substrate profiles amassed for various enzymes. These profiles have been used to construct active site models for such enzymes as pig liver esterase (PLE) (EC 3.1.1.1) and the microbial lipases (EC 3.1.1.3) Pseudomonas cepacia lipase (PCL), formerly P.fluorescens lipase, Candida rugosa lipase (CRL), formerly C. cylindracea lipase, lipase SAM-2 from Pseudomonas sp., and Rhizopus oryzae lipase (ROL) [108-116]. In addition, x-ray crystal structure information on PCL and CRL has been most helpful in predicting substrate activities and isomer preferences [117-119]. 

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