Candida lipase

Boldine, 2,9-diacetyl- Ester hydrolysis Candida lipase 199... 

In the enzymatic part of the process, a one-pot conversion was achieved by using Candida lipase (Lip) to hydrolyze the ester and then LeuDH to catalyze the reductive amination (with or without N labeling). In this case, the coenzyme recycling was accomplished by adding FDH and formate. The same group used a similar enzymatic strategy to prepare labeled L-threonine and L-allothreonine starting from the a-keto methyl ester. ... 

Steytler appears to be the only author who reports increasing reaction rates with increasing pressure at constant substrate concentration (mol/volume). They obtained higher conversion rates with increasing pressure from 150 bars to 300 bar in a Candida lipase B-catalyzed esterification in CO2 [54]. Further pressure increase to 500 bar did not result in any further rate increase. They speculate that the lower reaction rate at 150 bar may be due to adsorption of the ester on the enzyme bed. 

As a rule of thumb, the most widely used lipases may be characterized according to the steric requirements of their preferred substrate esters (Fig. 2.13). Whereas Aspergillus sp. lipases are capable of accepting relatively bulky substrates and therefore exhibit low selectivities on narrow ones, Candida sp. lipases are more versatile in this regard. Both the Pseudomonas and Mucor sp. lipases have been found to be highly selective on substrates with limited steric requirements and hence are often unable to accept bulky compounds. Thus, substrates which are recognized with moderate selectivities by a Candida lipase, are usually more... 

Acylsucioses (19) have become available for the first time by the chemoenzymatic procedure shown in Scheme 3. The I -butanoate and the 6,r-dibutanoate of sucrose were prepared by enzyme-mediated ester transfer from 2,2,2-trifluoroethyl butanoate in anhydrous pyridine, but the analogous reaction with 2,2,2-trifluoroethyl adipate showed little regioselectivity. Exposure of peracetylated sucrose to lipase OF, alcalase, Candida lipase, or chymotripsin caused preferential hydrolysis at 0-6, 0-1, 0-4, and 0-6, respectively, giving the various heptaacetates as the main products, whereas hydrolysis by a Pseudomonas lipase afforded a mixture containing the 2,3,4,6,l, 3, 6 -heptaacetate and the 23>4,6,3, 6 -hexaacetate in 20 and 41% peld, respectively. ... 

Similarly, symmetric sTAG rich in docosahexaenoic acid (DHA) at the sn-2 position and caprylic acid at the sn-l,3 positions can be obtained (Irimescu et al., 2001). Bonito oil was used as the substrate for ethanolysis, and the reaction was catalysed by Candida antarctica B lipase. After 2 h, a 92.5% yield of 2-MAG was obtained containing 43.5% DHA. After removal of the Candida lipase, Lipozyme RMIM was added directly without purification of the 2-MAG, and a final yield of 51% (w/w) sTAG was reported. 

HYDROLYSIS OF OILS AND FATS WITH CANDIDA LIPASE... 

Candida lipase was found to remove selectively the 6-0-acetyl group from methyl 2,3, -41 6-tetra-O-acetyl-a -D-glucopyranoside and the 5-0-butanoyl group from 3-0-acetyl-1,2-0-isopropylidene-5-0-butanoyl-x-D-xylofuranose. Secondary debutanoylation was also achieved on 5-0-2,2-dimethylpropanoyl-1,2-0-isopropylidene-3-0-butanoyl-o<-D-xylo-furanose using Candida lipase. Reversal of the normal action of lipases has been achieved in dry organic solvents when selective acylations at secondary positions were possible. Dibutylstannyl-idene acetal activation of the 2,6-dideoxy-hexopyranosides (1) - (3)... 

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