Lipase formerly Candida

Lipase ANL, lipase from Aspergillus niger, BCL, lipase from Burkholderia cepacia (formerly Pseudomonas cepacia) CAL-B, lipase from Candida antarctica B PPL, lipase from Pseudomonas fluorescens PPL, pig pancreatic lipase. 

As increasing research has been carried out with these enzymes, a less empirical approach has been taken as a result of the different substrate profiles that have been compiled for various enzymes in this class. These profiles have been used to construct active site models for such versatile enzymes as the carboxylester hydrolase, pig liver esterase (PLE) (E.C. 3.1.1.1), and the microbial lipases (E.C. 3.1.1.3) from Burkholderia cepacia (formerly Pseudomonas cepacia) lipase (PCL), Candida... 

Lipase (Candida rugosa formerly Candida cylindra-cea) Produced as an off white to tan powder by controlled fermentation using Candida rugosa. Soluble in water, but practically insoluble in alcohol, in chloroform, and in ether. Major active principle lipase. Typical applications used in the hydrolysis of lipids, in the manufacture of dairy products and confectionery goods, and in the development of flavor in processed foods. 

Lipase (Aspergillus niger var.), 20 Lipase (Aspergillus oryzae var.), 20 Lipase (Candida rugosa formerly Candida cylindracea), 20 Lipase (Rhizomucor (Mucor) miehei), 20... 

Lipase [(Candida rugosa) (formerly Candida cylindracea)], 132, 787, (S3)20... 

When Candida rugosa lipase (formerly named Candida cylindracea lipase) was immobilized on an epoxy-activated resin it became resistant against acetaldehyde. Due to this immunization it could be repeatedly employed for the enantioselective acylation of secondary alcohols with vinyl acetate in dry organic solvents (Scheme 2.7) [78]. 

Lipase Origin Candida rugosa (formerly C. cylindracea)... 

Hydrolases, especialy lipases, are noted for their tolerance of organic solvents, and are obvious candidates for the enzymatic synthesis in ILs (Sureshkumar Lee, 2009). Indeed, lipases from Candida antarctica, Burkholderia cepacia (formerly Pseudomonas cepacia), and Alcaligenes sp. are catalytically active in ILs (Itoh et al, 2001 Nara et al., 2002). Additionally, lipases mediate transesterification reactions in these ILs with an efficiency comparable to that in tert-butyl alcohol, dioxane, or toluene (Lau et al., 2000 Nara et al., 2002 Park Kazlauskas, 2001). 

Wild-type or engineered proteases and lipases were also foimd to catalyze aldol additions. First, examples were reported about the self-aldol addition of a,p-unsaturated aliphatic aldehydes (140) catalyzed by Pseudozyma antarctica lipase B (PalB) (formerly Candida antarctica CALB lipase) S105A and S105G variants (Scheme 10.34) [203,204]. The PalB S105A variant was also reported to catalyze aldol... 

In addition to cutinases, various lipases, such as from C. antarctica, Candida sp. [13, 47], Thermomyces lanuginosus [2, 14, 15, 55, 56], Burkholderia (formerly Pseudomonas) cepacia [57] and esterases from Pseudomonas sp. (serine esterase) [58] and Bacillus sp. (nitrobenzyl esterases) [59, 60], have shown PET hydrolase... 

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]. 

Unfortunately, X-ray structures are available only for a few enzymes, such as ot-chymotrypsin [116], subtilisin [181], and a number of lipases from Mucor spp. [9], Geotrichum candidum [332], Candida rugosa (formerly cylindracea) [333], Candida antarctica B [334], and Pseudomonas glumae [335] - while for a large number of synthetically useful enzymes such as pig liver esterase, relevant structural data are not available. 

Hydrolases such as lipases and proteases have been employed as the resolution catalysts for DKR. They include Candida antarctica lipase A (CAL-A), C. antarctica lipase B (CAL-B), Burkholderia (formerly Pseudomonas) cepacia lipase (BCL), Pseudomonas... 

The most common limitation for the enantioselective synthetic methods is poor enantio-selectivity. Crude Candida rugosa (CRL, formerly known as C. cylindracea) commercial lipase, one of the most used enzymes for the resolution of racemates, only exhibits poor to moderate enantiodiscrimination for the resolution of some racemic 2-arylpropionic acids and their derivatives (see Table lA). This might be due to the presence of other proteinaceous impurities (hydrolases and proteases with MW < 62 kDa) in the crude preparation [118], which may display opposite or poor enantioselectivity. A similar situation has also been described for crude lipase from pig pancreas [119]. 

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