Lipase Candida cylindracea

It has been demonstrated that the activity of the lipase Candida cylindracea) catalyzed transesterification reaction between methylmethacrylate and 2-ethylhexanol in... 

To find a suitable enzyme to catalyze the transesterification reaction (methyl ester to glycerol ester) under mild conditions, we screened a number of lipases and esterases. We found two lipases (Candida cylindracea lipase and porcine pancreatic lipase) to exhibit catalytic activity for this reaction. The reaction conditions entailed elevated temperatures, with the use of glycerol as the solvent and an acyl acceptor. The enzyme catalyzed the esterification of the carboxyl group of the pectin to the Cl (primary) alcohol of the glycerol to form the monoester. No substantial glycerol... 

Table 11.1-23. Lipase-catalyzed enantiomer- and enantiotopos-differentiating alcoholysis of carboxylic acid esters and anhydrides, alcoholysis or hydrolysis of oxazolin-2-ones, and esterification of carboxylic acids (PPL pig pancreas lipase, PCL Pseudomonas cepacia lipase, ANL Aspergillus niger lipase, CSL Candida sp. lipase, Candida cylindracea lipase, CAL-B Candida antarctica B lipase, CRL Candida rugosa lipase).

A soln. of rac. ethyl a-chloropropionate and -butylamine in hexane treated with yeast lipase Candida cylindracea), and stirred at 2° for 3 h - (S)-N-butyl-a-chloro-propionamide. Y 62% (e.e. 95%). F.e. and with aromatic amines s. V. Gotor et al.. Tetrahedron Letters 29, 6973-4 (1988). 

Candida cylindracea, phosphate buffer pH 7, Bu20. The 6-0-acetyl of Q -methyl peracetylglucose was selectively removed. Porcine pancreatic lipase will also hydrolyze acetyl groups from carbohydrates. These lipases are not specific for acetate since they hydrolyze other esters as well. In general selectivity is dependent on the ester and the substrate. ... 

Candida cylindracea lipase, BuOH, hexane, 3 h, 25°, 40-100% yield. 

Williams and coworkers have reported a DKR of ot-bromo [56a] and a-chloro esters [56b]. In the latter case, the KR is catalyzed by commerdally available cross-linked enzyme crystals derived from Candida cylindracea lipase. The racemization takes place through halide 5 2 displacement. The DKR is possible because the racemization of the substrate is faster than that of the produd (carboxylate). For the ester, the empty ii (C=0) orbital is able to stabilize the Sn2 transition state by accepting... 

The resolution of racemic ethyl 2-chloropropionate with aliphatic and aromatic amines using Candida cylindracea lipase (CCL) [28] was one of the first examples that showed the possibilities of this kind of processes for the resolution of racemic esters or the preparation of chiral amides in benign conditions. Normally, in these enzymatic aminolysis reactions the enzyme is selective toward the (S)-isomer of the ester. Recently, the resolution ofthis ester has been carried out through a dynamic kinetic resolution (DKR) via aminolysis catalyzed by encapsulated CCL in the presence of triphenylphosphonium chloride immobilized on Merrifield resin (Scheme 7.13). This process has allowed the preparation of (S)-amides with high isolated yields and good enantiomeric excesses [29]. 

Various cyclic esters have been subjected to hpase-catalyzed ring-opening polymerization. Lipase catalyzed the ring-opening polymerization of 4- to 17-membered non-substituted lactones.In 1993, it was first demonstrated that medium-size lactones, 8-valerolactone (8-VL, six-membered) and e-caprolactone (e-CL, seven-membered), were polymerized by lipases derived from Candida cylindracea, Burkholderia cepacia (lipase BC), Pseudomonas fluorescens (lipase PF), and porcine pancreas (PPL). °... 

Stirred-tank reactor Alcoholysis of 1-phenyl ethyl butyrate and 1-heptanol Lipase from Candida cylindracea 120... 

A continuous stirred tank reactor has been reported for the hydrolysis of the triglycerides existing in vegetable oil in the presence of the aqueous phase and for synthesis reactions (Table 5). A microfilter can be used to prevent the immobilized enzyme from leaving the reactor. Kawano et al. [115] investigated the hydrolysis of olive oil in octane with Candida cylindracea lipase in aqueous solution in a Vibro Mixer reactor containing vibration plates connected to the crankshaft of a motor and oscillated with fixed rates. 

Enantiomerically pure japonilure [(4JR,5Z)-5-tetradecen-4-olide, 26] is commercially important to attract the Japanese beetle (Popillia japonica), because only pure (4.R,5Z)-26 is bioactive, while ( )-26 is totally inactive. Synthesis of (4 ,5Z)-26 via enzymatic resolution of racemic intermediates was first reported by Sugai [63], and then further studied by Fukusaki [64] to establish the process as summarized in Scheme 39. Lipase PS (Amano) from Pseudomonas sp. and lipase OF (Meito) from Candida cylindracea were shown to be the enzymes of choice. 

Enzyme activity varies greatly depending on solvent choice, as illustrated by Zaks and Klibanov for the transesterification of tributyrin and heptanol by three different lipases. Using these data, Laane et found that enzyme activity correlates closely with solvent hydrophobicity (log P) for the lipases from Mucor sp. (MML) and Candida cylindracea... 

CCL lipase from Candida cylindracea (now known as lipase from... 

To test the selectivity of the self-screening process, six other enzymes belonging to the hydrolase family were tested under the same set of conditions as in DCL-A. These enzymes were butyrylcholinesterase, horse fiver esterase (HLE, EC 3.1.1.1), Candida cylindracea lipase (CCL, EC 3.1.1.3), (3-galactosidase ((3-Gal, EC 3.2.1.23), trypsin (EC 3.4.21.4), and... 

Rua, M L., Diaz-Maurino, T. Fernandez, V.M., Otero, C. and Ballesteros, A. (1993) Purification and partial characterization of two distinct lipases from Candida cylindracea. Biochim. Biophys. Acta., 1156, 181-189. 

Kinetic optical resolution of racemic alcohols and carboxylic acids by enzymatic acyl transfer reactions has received enormous attention in recent years56. The enzymes generally employed are commercially available lipases and esterases, preferentially porcine liver esterase (PLE) or porcine pancreatic lipase (PPL). Lipases from microorganisms, such as Candida cylindracea, Rhizopus arrhizus or Chromobacterium viscosum, are also fairly common. A list of suitable enzymes is found in reference 57. Standard procedures are described in reference 58. Some examples of the resolution of racemic alcohols are given39. 

Lipases (triacyl glycerol acyl hydrolases, E.C 3.1.1.3) are a unique class of hydrolases for asymmetric synthesis86,87,S9,90e, They are available from fungi, bacteria and mammalians. The lipases most commonly used so far are the commercially supplied pig pancreas lipase (PPL)136, Pseudomonas cepacia lipase (PCL)89,137 and Candida cylindracea lipase (CCL). In most cases only the crude lipases, consisting of a mixture of proteins which may even be other hydrolases, are successfully applied1373. 

It is known that enantioselectivity of enzymes depends on many different parameters such as temperature, substrate structure, reaction medium, and presence of water. Enantiopreference of enzymes can be greatly affected, even reversed, by changing the reaction solvent. Such an example was reported by Ueji et al. in 1992 for Candida cylindracea lipase-catalyzed esterification of ( )-2-phenoxy propionic acid with 1-butanol [29]. 

If the bonded water is extracted by dry CO2 the enzyme is denaturated and loses its activity. Therefore a certain amount of water is necessary in the supercritical fluid because acting with water-saturated CO2 again causes an inhibition of the enzyme and consequent loss of activity. The optimal water concentration has to be determined for each enzyme separately. Table 9.2-1 shows the residual activity of lipase from Candida cylindracea, esterase from Mucor mihei, and esterase from Porcine liver after a incubation time of 22 hours in supercritical CO2 at 40°C. It is obvious that higher water concentrations cause a strong reduction in the residual activity compared to the activity of the untreated enzyme, which was set as 100 %. Further, the system-pressure has an influence because at higher pressures the activity-loss is lower with a larger amount of water in the system [7,8],... 

Residual activity at different CO2 humidity at 40°C, 22 hours incubation time and 170 mL total volume of the system (I, lipase from Candida cylindracea II, esterase from Mucor mihev, III, esterase from Porcine liver) ... 

Residual activity of different enzymes after 1 hour treatment in supercritical CO2 at 150 bar (I, lipase from Candida cylindracea If, lipase Amano AY III, lipase from Pseudomonas sp. IV, esterase EP10 from Burkholderia gladioli) ... 

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

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