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PublicationJournal of Chemical Technology & Biotechnology

Ethyl butyrate synthesiscatalyzed by lipase B from Candida antarctica: optimal conditions depend on the immobilization protocol

Authors:John L. R. Friedrich , Fernanda P. Peña, Cristina Garcia-Galan, Roberto Fernandez-Lafuente, Marco A. Z. Ayub , Rafael C. Rodrigues
Groups of research:Optimization of biocatalysts and bioprocesses
In this work it has been compared two immobilized preparations of lipase B from Candida antarctica (CALB) as biocatalysts in the synthesis of ethyl butyrate, a short-chain esters with fruity notes. Commercial Novozym 435 and CALB immobilized on styrene-divinylbenzene beads (MCI-CALB) were tested in the esterification reaction, and reaction temperature, substrate molar ratio, enzyme content and added water were optimized using an central composite design and the response surface methodology. The acid concentration that permitted the maximal initial reaction rate was determined to be 0.7 M. Both preparations presented different optimal condition regarding the ethyl butyrate production. Optimal reaction temperature and substrate molar ratio were different for each biocatalyst while enzyme content and added water were the same. At optimal condition it was possible to obtain a yield around 85% in 1.5 h. However MCI-CALB presented a productivity 1.6-fold higher than Novozym 435. The main difference between both biocatalysts was in relation to operational stability. Performing a n-hexane washing before each batch reuse, Novozym 435 presented 20% of its initial activity after 8 batches while MCI-CALB retained 80% of its initial activity. 
Keywords:ethyl butyrate; flavour esters; CALB; esterification; RSM; enzyme reuse
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