Comparison of the performance of entrapped and covalently immobilized lipase in the synthesis of pear flavor

Abstract

Introduction:Although aroma esters are produced mostly by a chemical method that requires the use of aggressive chemical catalysts, enzymatic esterification has been very favored during previous two decades. The main aim of this study was to investigate the commercially important pear flavor, hexyl acetate (HAc), by the catalysis of immobilized lipase samples and to optimize the immobilization and operational conditions in detail.Methods:Lipases fromResults:Among the several organic media, the highest esterification activites were observed in heptane. HAc yield decreased when substrate concentrations were higher than 50 or 75 mM. Yield increased with increase in reaction time up to the 5Discussion and conclusions:As well as synthesis conditions, immobilization parameters also affected HAc productivity. The amount of water in the microenvironment of lipase is so important not only for gaining its active conformation but only for the reaction direction.

Enzyme immobilization: what have we learned in the past five years?

“…Lipase was also one of the most frequent words in the review of Gonçalves et al 15 Laccases find application in antibiotic synthesis, 161 phenolic compound elimination, 162 water purification, 163 bioremediation 164 and industrial dye degradation. 165 Lipases are mainly used for biodiesel production, 166 oil hydrolysis 167 or esterification 168 and the production of flavor 169 and aroma esters. 170 In summary, studies on enzyme immobilization cover a variety of topics, including support development, different immobilization methods and the use of different enzymes associated with several processes.…”