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Application L2417

Intrinsic Kinetics Resolution of an Enantioselective Transesterification Catalyzed with the Immobilized Enzyme Novozym 435

Nicolas Chaussard, Clémence Nikitine, Pascal Fongarland

ACS Eng. Au 2024, 4, 6, 545–561

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"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 additional estimation of the internal mass transfer using an orthogonal collocations method. A total of 18 experiments (774 data points) were conducted in the SpinChem Vessel V2 batch reactor at a constant stirring speed of 400 rpm, varying temperatures, initial molar fractions, catalyst ratio, and size fraction. Kinetics data were fitted using the model, resulting in optimized kinetic parameters, which align with expected Ping-Pong Michaelis-Menten mechanisms. Values for the effectiveness factor for intraparticle mass transfer diffusion vary between 0.37 and 1, indicating the need to include mass transfer considerations in kinetic modeling."

Keywords

#kineticmodeling, #transesterification, #MichaelisMenten, #Novozym435, #enzymaticreaction, #massTransfer

 

SpinChem RBR S2 rotating bed reactor and Vessel V2 experimental setup with labeled components including mechanical stirrer, sampling ports, catalyst agitator, and draining valve.


Application L2417 SpinChem RBR S2 and Vessel V2 Experimental Setup

 

L2417 Effect of Stirring Speed on Transesterification Conversion in SpinChem RBR

 

Highlights:

  • The study demonstrates the effectiveness of the SpinChem RBR S2 + Vessel V2 in facilitating enantioselective transesterification reactions catalyzed by Novozym 435.
  • Using a Ping-Pong bi-bi model, researchers examined the reaction rates with considerations for internal mass transfer.
  • “External mass transfer limitations were found nonlimiting for stirring speeds higher than 400 rpm"
  • This research highlights the importance of the role of the SpinChem reactor in supporting sustainable, scalable processes in biocatalysis.

Authors & Research Group

This research was conducted by the Laboratory of Catalysis, Polymerization, Processes and Materials (CP2M) at Université Claude Bernard Lyon 1 and CPE Lyon in Villeurbanne, France, bringing together expertise in catalysis, enzymatic reaction engineering, and process intensification.

Nicolas Chaussard (LinkedIn) 

Clémence Nikitine (LinkedIn)

Pascal Fongarland (LinkedIn)

SpinChem perspective: industry applications

This study demonstrates that the rotating bed reactor can eliminate external mass transfer limitations which is critical for cost-effective scale-up. With the stirring speed set to only 400 rpm in the benchtop reactor, the kinetics became independent of further increasing the speed. This effective elimination of mass transfer limitations translates to energy savings on industrial scale, as well as predictable performance when scaling up.

What makes enzyme reusability economically viable?

The immobilized enzyme format and convenient recycling of the biocatalyst in the rotating bed reactor allow companies to maximize the benefits gained from their enzyme inventory, reduce waste generation, and lower operational costs. This unlocks the economic benefits of immobilized enzymes at production scale.

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Topics Scientific Literature, Biocatalysis

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