Activities in ester synthesis

The activities of immobilized C. antarctica and Mucor lipases in ester synthesis of propanol and isopropanol were compared (Fig. 8) Both lipases have high activities in ester synthesis with the primary alcohol propanol, but only the positional non-specific C. antarctica lipase performs well in synthesis with the secondary alcohol. 

Even though the immobilized Lipase B has lew activity in acidolysis, it is quite active in ester synthesis with short-chain alcohols where it seems to be responsible for the abilities shewn by the crude enzyme. Lipase B functions almost equally well on 1-propanol and 2-propanol but for the long-chain alcohol, oleic alcohol, Lipase B has somewhat lower activity, and Lipase A seems to contribute the activity observed for the crude enzyme. 

In contrary to Lipase B, Lipase A has lew activity in ester synthesis with short chain alcohols, and higher activity on long chain alcohols. 

Lipase A seems to be responsible for the interesterification characteristics of the immobilized crude lipase preparation, including its unique specificity towards saturated fatty acids. Further, Lipase A can explain some of the activity found in ester synthesis with long-chain alcohols. On the other hand, Lipase B is responsible for the activity in ester synthesis of short-chain alcohols, and for some of the activity on long-chain alcohols. 

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See also in sourсe #XX -- [ , ]

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