In this work was optimized the production of benzyl cinnamate by enzymatic catalysis using the immobilized lipase NS88011 and to evaluate its biological properties. The optimized condition for this system was 1:3 (acid:alcohol) molar ratio, 59 °C, biocatalyst concentration 4.4 mg.mL-1 for 32 h, with a yield of 97.6 %. The enzyme stability study showed that the enzyme remains active and yields above 60 % until the 13th cycle (416 h), presenting a promising half-life. In the determination of the antioxidant activity of the ester, an inhibitory concentration necessary to inhibit 50 % of the free radical 2,2-diphenyl-1-picryl-hydrazyl DPPH (IC50) of 149.8 mg.mL-1 was observed. For acute toxicity against bioindicator Artemia salina, lethal doses (LD50) of 0.07 and 436.7 μg.mL-1 were obtained for the ester and cinnamic acid, showing that benzyl cinnamate had higher toxicity, indicating potential cytotoxic activity against human tumors.
Keywords: Enzymatic esterification; Lipase NS 8801; Operational cycle; Optimization.
© 2021 The Authors. Published by Elsevier B.V.