GERANYL CINNAMATE ENZYMATIC SYNTHESIS APPLYING NS88011 LIPASE WITHIN A BATCH STIRRED TANK REACTOR

Geranyl cinnamate (GC) is an FDA-approved compound used as a natural flavoring agent with added benefits of antimicrobial and antioxidant properties. GC is typically synthesized through chemical or enzymatic catalysis using lipases. In this study, NS88011 was applied, a cost-effective commercial lipase, that offers a competitive advantage over alternatives. The objective of this work was the production of GC ester through enzymatic esterification using the commercial lipase NS88011. A batch stirred tank reactor (BSTR) was employed with the enzyme and its substrates being geraniol (acyl donor) and cinnamic acid in a 3 h reaction. A central composite design (CCD) 2³ was used to maximize the conversion to geranyl cinnamate. The independent variables studied were temperature (50 to 80 ºC), molar ratio of cinnamic acid to geraniol (1:3 to 1:5), and enzyme concentration (5 to 15% w/w). The independent variables were statistically significant (p < 0.05) in the conversion of geranyl cinnamate, and with the assistance of the Protimiza® software, a mathematical model was obtained that fit the experimental data well (R² = 94.08%); ANOVA was also performed using the software to assess the suitability of the proposed model. The analysis yielded an F-value (71.6) higher than the critical F-value (2.93), indicating that the polynomial model obtained accurately describes the synthesis of geranyl cinnamate under the studied conditions. NS88011 provided the best results (51.89% w/w conversion of substrates to ester) under the highest conditions of temperature (80 ºC) and enzyme concentration (15%) studied, as well as at a higher molar ratio of cinnamic acid to geraniol (1:5) in 3 h reaction. The effective use of commercial lipase NS88011, along with statistical analysis, highlights the potential to improve yield, cost-efficiency, and environmental sustainability in producing a compound with growing importance in the food sector.