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On the positional and chain specificities of Candida cylindracea lipase

1971; Elsevier BV; Volume: 231; Issue: 1 Linguagem: Inglês

10.1016/0005-2760(71)90251-7

1879-145X

Gilbert Benzonana, Simone Esposito,

Microbial Metabolic Engineering and Bioproduction

The lipase (EC 3.1.1.3) from the microorganism Candida cylindracea is very active on long chain triglycerides at pH 8.0 and 37°. Under these conditions the three chains of the glycerol moiety are hydrolyzed. Free glycerol appears in the same time as the other reaction products, however, monoglycerides are present only in very minute amounts, all along the course of lipolysis. It can thus be supposed that the enzyme is able to hydrolyse all the ester bonds of the glycerol. A comparison between the proportions of the fatty acid chains in intact olive oil and cocoa butter and the proportions of fatty acids liberated after a limited hydrolysis of these lipids shows that the lipase of Candida liberates all types of acyl chains, regardless of their position in the glycerol. However, palmitic and oleic chains are liberated before stearic acid when they are present together in a given glyceride. When synthetic glycerides, containing only palmitic and oleic acid chains, are submitted to a partial lipolysis by Candida lipase, the composition of the liberated fatty acids and the composition of the acyl chains in the intact triglycerides are similar. However, oleic acid is liberated before palmitic acid, regardless of their respective position, as would appear from the composition of diglycerides and monoglycerides. Since 1,3-dihexadecyl-ether-2-oleoyl-glycerol is readily hydrolyzed it can be concluded that the Candida lipase is able to attack secondary ester groups of glycerol without the help of an isomerase.