Production of benzyl cinnamate by a low-cost immobilized lipase and evaluation of its antioxidant activity and toxicity.
Ontology highlight
ABSTRACT: 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 dose
SUBMITTER: Piazza SP
PROVIDER: S-EPMC7809389 | biostudies-literature | 2021 Mar
REPOSITORIES: biostudies-literature
ACCESS DATA