CRL Candida rugosa lipase

Fig. 5.13. Lipase-catalysed hydrolysis of racemic ibuprofen ester. CRL Candida rugosa lipase.

Table 11.1-11. Lipase-catalyzed enantiotopos-differentiating hydrolysis of prochiral cyclic diol dialkanoates in aqueous solution (CCL Candida cylindracea lipase, PFL Pseudomonas jiuorescens lipase, MML Mucor miehei lipase, CVL Chromobacterium viscosum lipase, PPL pig pancreas lipase, MJL Mucor javanicus lipase, RSL Rhizopus sp. lipase, PCL Pseudomonas cepacia lipase, CCL, Ceotricum candidum lipase, ANL Aspergillus niger lipase, FSPC Fusarium solani pisi cutinase, CRL Candida rugosa lipase, CAL-B Candida antarctica B lipase, LIP Pseudomonas sp. lipase-Toyobo, RDL Rhizopus delemar lipase, MSL Mucor sp. lipase, CAL Candida antarctica lipase, not specified).

Table 11.1-16. Lipase-catalyzed enantiomer-differentiating hydrolysis of esters of racemic cyclic secondary and tertiary alcohols in aqueous solution (PFL Pseudomonasfluorescens lipase, PSL Pseudomonas sp. lipase, CCL Candida cylindracea lipase, ABL Arthrobacter sp. lipase, PCL Pseudomonas cepacia lipase, CRL Candida rugosa lipase, CE cholesterol esterase).

Layered phosphate/phosphonate and phosphonate materials, obtained by substitution of the phosphate moiety by phosphonate groups, display interesting tunable hydrophilic/organophilic properties for adsorption processes. When Candida rugosa lipase (CRL) is simply equilibrated with zirconium phosphate and phosphonate [135,136], immobilization was demonstrated to take place at the surface of the microcrystals. However, because lipase exhibits a strong hydrophobic character, its uptake by zirconium phosphate and phosphonate was much more related to the hydrophobic/hydrophilic character of the supports than to the surface area properties. A higher uptake is observed for zirconium-phenylphosphonate (78 %)... 

The cutinase from Fusarium solani pisii maintained its transesterification activity in [BMIm][BF4], [OMIm][PF6] and [BMIm][PF6] (in order of increasing activity) at aw=0.2 [59]. Candida rugosa lipase (CrL), which is generally much less tolerant of anhydrous media than other microbial lipases, has successfully been used in anhydrous as well as water-saturated ionic liquids [60, 61, 62, 63, 64, 65]. 

Inlet Figure Crystal structure of Candida rugosa lipase (CRL, E.C. 3.1.1.3), complexed with (lS)-menthyl hexyl phosphonate (Cygler, 1994). 

Figure 2 Stability of (A) CRL-CLEC and (B) commercial CRL (inset) in the presence of water-miscible organic solvents. The catalyst was stored in the presence of 50% aqueous solvent at 25°C. CRL is Candida rugosa lipase. (Reproduced from Ref. 16. 1995 American Chemical Society.)...

As well as the kinetic resolution of chiral alcohols, lipases can be employed to resolve chiral acids. Their enantioselectivity towards chiral acids or their esters is, however, less predictable. Candida rugosa lipase (CRL) has a general stereochemical preference for one enantiomer of acids with a chiral a-carbon (Scheme 6.4) [15]. 

Candida rugosa lipase (CRL) hydrolysed the other enantiomer selectively (Scheme 6.11). This proves once again that in most cases enzymes with the desired stereoselectivity are available. 

CAL (Novozym 435) Candida antarctica) QL Alcalgenes sp.) PS (Psedomonas cepacia Amano lipase PS) CRL Candida rugosa Meito lipase OF) PPL Porcine liver lipase (Sigma Type II). 

In addition, Itoh and coworkers have reported that acylation of the alcohol was accomplished by three types of enzymes Candida Antarctica lipase (CAL, Novozym 435), lipase QL Alcalgenes sp.), and lipase PS Pseudomonas cepacia). Scheme 10.5. The desired acetate showed extremely high enantioselectivity, but no reaction took place when lipase (CRL, Candida rugosa) or Procine liver lipase (PPL) was used as the catalyst in the ionic liquid (Table 10.3). 

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]. 

Even though CaLB is the lipase most widely used in ionic liquids, other lipases such as Pseudomonas cepacia lipase (PcL) and Candida rugosa lipase (CrL) have been often used as biocatalyst for ester synthesis in ionic liquid [13, 14]. Nara et al. 

A related selectivity-enhancing noncovalent modification of Candida rugosa lipase, which does not require tedious protein chromatography and which is therefore applicable to large-scale reactions is based on the treatment of crude CRL with 50% aqueous wo-propanol, which led (after simple centrifugation and dialysis) to a modified lipase preparation, which was not only more active, but also showed considerably enhanced enantioselectivity [424],... 

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