Novozym 40086 as a novel biocatalyst to improve benzyl cinnamate synthesis

Abstract

Benzyl cinnamate is one of the derivatives of cinnamic acid, which can be used as the main constituent in perfume, UV filters and medicines. In this work, several commercial immobilized lipases (Novozym 40086, Novozym 435 and Lipozyme TLIM) and free lipases (lipase A and B from Candida sp., and lipozyme from Thermomyces linuginosous) were used as catalysts for benzyl cinnamate preparation by the esterification of benzyl alcohol with cinnamic acid. The effect of various esterification parameters (reaction time, reaction temperature, lipase concentration and substrate ratio) on benzyl cinnamate yield were also optimized and evaluated using response surface methodology (RSM). Among all tested lipases, Novozym 40086, as a new commercial immobilized lipase from Rhizomucor miehei immobilized on acrylic resin beads, showed the best activity for the esterification. Esterification parameters were optimized as follows: reaction temperature 46.3 °C, substrate molar ratio 1 : 3 (cinnamic acid/benzyl alcohol), Novozym 40086 concentration 23.1 mg mL−1, reaction time 11.3 h, and maximum benzyl cinnamate yield (96.2 ± 1.4%) were achieved under the optimal conditions. Novozym 40086 can be reused 9 times without significant decrease in benzyl cinnamate yield (90.1% yield after nine times). The activation energy for the Novozym 40086-catalyzed esterification was 14.96 ± 0.25 kJ mol−1. These results showed that Novozym 40086 was a novel and efficient biocatalyst for the esterification, which can be used as a good alternative for benzyl cinnamate production.