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Production and optimization of isopropyl palmitate via biocatalytic route using home‐made enzymatic catalysts

Barsé, Laísa Q, Graebin, Natália G, Cipolatti, Eliane P, Robert, Julia M, Pinto, Martina CC, Pinto, Jose CCS, Freire, Denise MG, Rodrigues, Rafael C
Journal of chemical technology and biotechnology 2019 v.94 no.2 pp. 389-397
Pseudozyma antarctica, biocatalysts, carboxylic ester hydrolases, cyclohexanes, enzyme activity, heptane, hexane, iso-octanes, isopropyl alcohol, palmitates, palmitic acid, solvents, statistical analysis, temperature
BACKGROUND: This study investigated the use of core–shell biocatalysts, synthesized using recombinant lipase B from Candida antarctica (CALB), for the production of isopropyl palmitate and the optimization of this biocatalytic route. RESULTS: Initially, three distinct core–shell biocatalysts, were evaluated for the production of isopropyl palmitate and the CALB‐P(S‐co‐DVB)/P(S‐co‐DVB) biocatalyst (biocatalyst made of polystyrene‐co‐divinylbenzene core–shell particles) was the most suitable biocatalyst for this purpose. The effect of organic solvents – n‐hexane, isooctane, n‐heptane and cyclohexane – in the ester conversion was evaluated, and the most suitable solvent was the isooctane. The optimal reaction conditions were pursued conducting an optimization statistical analysis. The most suitable reaction conditions were identified: reaction temperature, 55°C; substrate molar ratio, 1:1.42 (palmitic acid: isopropyl alcohol); biocatalyst content, 24% w/w. Finally, the reuse of the biocatalyst was evaluated and the relative enzymatic activity remained up to 50% after the fourth cycle. CONCLUSION: Results were compared with commercial biocatalyst and the home‐made enzymatic biocatalyst (CALB‐P(S‐co‐DVB/PS‐co‐DVB) showed promise for application in the synthesis of isopropyl palmitate. The optimization study improved reaction conversion from 30% to 78%. The home‐made biocatalysts exhibited better performance for the synthesis of isopropyl palmitate compared with the commercial Novozym 435, using the same enzymatic activity. © 2018 Society of Chemical Industry