Enzymatic processes

Development and modeling of enzymatic processes

We study bioreactors with free or immobilized enzymes for applications in the food and biotechnology field. The approach used is based on the principles of unit operations and processes (mass balances, chemical and enzyme kinetics, mass transfer effects, enzyme deactivation and inhibition phenomena). 

Acid urease from Lactobacillus fermentum is of interest in the alcoholic beverage industry to reduce the concentration of urea, the precursor of ethylcarbamate. We have studied this enzyme extensively.
More recently, we developed urease-immobilized porous media. The immobilized particles have been applied in fixed-bed and mechanical stirred bioreactors for detoxification of various wines. In parallel, mathematical models have been developed to describe the reactors using reaction-diffusion models implemented using COMSOL Multiphysics simulation software.

Another research activity involved the production, purification and immobilization of the enzyme L-arabinose isomerase for the conversion of D-galactose to D-tagatose. The obtained biocatalyst was kinetically characterized and used in fixed-bed reactors. Protocols for stabilization of the immobilized enzyme have also been developed. The aim is to apply such a biocatalyst in the isomerization of D-galactose, obtainable from lactose in whey, into D-tagatose, a rare sugar of considerable food and pharmaceutical interest.

We have recently started to study the enzymatic hydrolysis of proteins by trypsin to obtain peptides for applications in the food and pharmaceutical fields.