Roberto Fernandez-Lafuente holds a degree in Biology from Universidad Complutense de Madrid, a Ph.D in Sciences from Universidad Autónoma de Madrid and a Post doctorate from University College London. He is presently the lead researcher responsible for the group "Optimization of bioprocesses and biocatalysis" at ICP-CSIC and have a position as Full Professor.
He has experience in the study of the interactions between biomacromolecules and activated solids, either to purify or immobilize/stabilize these biomacromolecules. Moreover, he has expertise in the chemical and physical modification of these biomacromolecules, either to improve their properties or to improve their immobilization. The prepared biocatalysts are used in diverse processes, from oxidations to hydrolysis, from biodiesel production to hydrolysis of proteins, etc. He has coauthored over 550 papers and 20 patents, and has supervised 24 doctoral theses, presenting a H-index of 94 (scopus), being included in the Clarivate HCR lists in 2019, 2020 and 2021.
Enzyme co-immobilization: advantages, necessity, problems and solutions
The coimmobilization of enzymes is everyday most popular. This is related to the current interest for cascade reactions. The enzyme coimmobilization offers some kinetic advantages, mainly related to a significant increment of the initial reaction rates due to the production of the intermedia products in confined spaces, which makes that all the enzymes from the cascade can act on high, even saturating concentrations (in some instances), of their respective substrate from the beginning of the reaction. This reduces or eliminates the usual lag time observed in cascade reactions. In some instances, the existence of this lag time can make the process unsuitable, making coimmobilization fully necessary. However, enzymes coimmobilization has diverse drawbacks at different levels, being the possibility of using enzymes with very different stabilities the one where we will focus in this conference. Some solutions for preparing coimmobilized enzymes where the most stable immobilized enzyme can be reutilized for the preparation of a new combienzyme will be briefly presented, All the strategies will be coupled to the combined use of different immobilization protocols (being at least one reversible, to selectively release the inactivated less stable enzyme).