engleski

Mathematical model development of enzyme catalyzed aldol addition

Carbon-carbon bond formation between propionaldehyde and formaldehyde using the thermostable D-fructose-6-phosphate aldolase as a green and enantioselective catalyst was investigated. The reaction kinetics can be described by the double substrate Michaelis- Menten kinetics with included substrate inhibitions by formaldehyde and propanal. Mathematical model for the reaction in the batch reactor included self-addition of propanal catalyzed by FSA also described by Michaelis- Menten kinetics. Experiment performed in batch mode shows that the mathematical model describes the experimental data well. Due to inhibition by both substrates high concentration of the product cannot be achieved. Also, high substrate concentration cannot be used due to their negative effect on enzyme stability. Based on the model for reaction in batch reactor, conditions for fed batch reactor were simulated in order to produce higher amount of aldol product. Fed batch mode suits this reaction system better than batch mode, and once optimized it will give the high product concentrations.

biocatalysis, aldol addition

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