Intrinsic Kinetics Resolution of an Enantioselective Transesterification Catalyzed with the Immobilized Enzyme Novozym435

• Published in: ACS Engineering Au Vol. 4; no. 6; pp. 545 - 561
• Main Authors: Chaussard, Nicolas, Nikitine, Clémence, Fongarland, Pascal
• Format: Journal Article
• Language: English
• Published: American Chemical Society 18.12.2024
• Subjects: Chemical and Process Engineering; Engineering Sciences; enantioselective enzymatic transesterification; orthogonal collocations; Michaelis–Menten kinetics; effectiveness factor; Novozym435; kinetic modeling
• ISSN: 2694-2488; 2694-2488
• DOI: 10.1021/acsengineeringau.4c00030

This work investigates the kinetics of the enantioselective transesterification of ethyl butyrate and (R)-2-pentanol in a solventless medium biocatalyzed by Novozym435, an immobilized Candida antarctica Lipase B. A reaction-diffusion reversible Ping-Pong bi-bi model was developed to represent the reaction rate with the additional estimation of the internal mass transfer using an orthogonal collocations method. A total of 18 experiments (774 data points) were realized in the SpinChem Vessel V2 batch reactor at a constant stirring speed of 400 rpm, varying temperatures (30–60 °C), component initial molar fraction (0.2–0.8), catalyst ratio (1–4% wt), and size fraction (200–1000 μm). Kinetics data were fitted using the model with a mean average percentage error of 3.45%, the 10 optimized kinetic parameters being coherent with the expected behavior of the Ping-Pong Michaelis–Menten mechanisms. Values for the effectiveness factor η for intraparticle mass transfer diffusion vary between 0.37 and 1, confirming the necessity to include mass transfer into kinetic modeling in our case.