Candida antarctica cylindracea

Candida antarctica (enantioselective) Candida cylindracea lipase (enantioselective)... 

The lipases most used until now are the commercially supplied pig pancreas lipase (PPL), Pseudomonas cepacia lipase (PCL) or P. Jluorescens lipase (PFL), Candida cylindracea (CCL) or C. rugosa lipase (CRL), Pseudomonas sp. lipase (PSL), increasingly Candida antarctica B lipase (CAL-B) and to a lesser extent further lipases mentioned in Tables 11.1-10 to 11.1-25, and cholesterol esterase (CE). CAL-B is a recombinant protein produced in AspergiUus oryzae accepting a broad range of substrates and conditions. A special group of hydrolases, which are considered as lipases, are the cholesterol esterases (CE), found in mammals and microorganisms1113. ... 

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).

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. 

Many lipases, such as porcine pancreatic lipase (PPL), Candida cylindracea lipase (CCL), Chromobacterium viscosum lipase (CVL), Candida antarctica lipase (CAL), Candida antarctica lipase B (CALB, Novozyme-435), polyethylene glycol (PEG)-modified Pseudomonas fluorescens lipase (PEL), Pseudomonas cepacia lipase (PsCL),... 

Another approach for the enzymatic preparation of 5-ibuprofen has been demonstrated by de Zoete et al. [229]. The enantioselective ammonolysis of ibuprofen 2-chlo-roethyl ester by Candida antarctica lipase (lipase SP435) gave the remaining ester 5-(+) enantiomer in 44% yield and 96% e.e. The enantioselective enzymatic esterification of racemic ibuprofan has also been demonstrated using lipase from Candida cylindraceae [230]. The reaction was carried out in a water-in-oil microemulsion [bis(2-ethyl-hexyl)sulfosuccinate (AOT)/isooctane). The lipase showed high preference for the S-(+) enantiomers of ibuprofen which was esterified and R-(—) enantiomer remained unreacted. The reaction yield of 35% was obtained using n-propanol in the reaction mixture as nucleophile. 

A series of acetoxy derivatives of androstane were deacylated in organic solvents by several lipases. The most satisfactory results were obtained with lipase from Candida cylindracea (CCL) and Candida antarctica (CAL). In some derivatives, CCL and CAL showed an overwhelming regioselectivity toward the removal of the 3p- or the IT -acetyl group and three new steroid derivatives were obtained [31] through this approach (Fig. 17). 

The possible application of enzyme-assisted reactions for production of lower value nonspecialty lipids such as margarine hardstocks and cooking oils has been reported (50). When nonspecific lipases, such as those from Candida cylindraceae and C. antarctica, are used as biocatalysts for interesterification of oil blends, the TAG... 

Several crude lipase preparations are available from the yeasts Candida lipolytica, C. antarctica (CAL), and C. rugosa (CRL, syn. C. cylindracea). The latter enzyme, the three-dimentional structure of which has been resolved by X-ray analysis [333], has been frequently used for the resolution of esters of secondary alcohols [401-406] and, to a lesser extent, for the resolution of a-substituted carboxylates [407,408]. The CRL preparations from several commercial sources which contain up to 16% of protein [409] differ to some extent in their activity but their selectivity is very similar [410]. As CRL is able to accommodate relatively bulky esters in its active site, it is the lipase of choice for the selective hydrolysis of esters of cyclic secondary alcohols. To illustrate this point, some representative examples are given below. 

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