Production of benzyl cinnamate by a low-cost immobilized lipase and evaluation of its antioxidant activity and toxicity

• Main Authors: Suelen Paloma Piazza, Bruna Maria Puton, Rogério Marcos Dallago, Débora de Oliveira, Rogério Luis Cansian, Marcelo Mignoni, Natalia Paroul
• Format: Article
• Language: English
• Published: Elsevier 2021-03-01
• Series: Biotechnology Reports
• Subjects: Optimization; Enzymatic esterification; Lipase NS 8801; Operational cycle
• Online Access: http://www.sciencedirect.com/science/article/pii/S2215017X21000023

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.