Structural behaviour of adsorbed/immobilised enzymes on planar interfaces

Characterizing the structural deformation of enzymes upon immobilization is of paramount importance as it directly impacts the efficiency and effectiveness of heterogeneous biocatalysts. Gaining a deeper understanding of these structural changes will guide the immobilization protocols to obtain more robust and active immobilized enzymes with a wide range of application in biotechnology, pharmaceutical, cosmetic and the food industry. Here we will investigate the structural rearrangements undergone by a model lipase from Candida Antarctica (CALB) immobilized on silicon functionalized with different functional groups (hydrophobic and hydrophilic ones). These structural rearrangements at the interface between the solutions of enzymes and the solid surface are hard to characterize by conventional techniques (circular dichroism, fluorescence spectroscopy, etc), however neutron reflectometry (NR) can give us unprecedent information with spatiotemporal information about the molecular process that occur when an enzyme is bound to a solid surface, and how these bound enzymes behaves under temperature stress. We expect that NR will help us to create a bridge between structure and function of immobilized enzymes to better understand the computational and kinetic results. We select CALB because this is one of the most widely used materials for industrial applications, fundamental to design and fabricate more active and robust heterogeneous biocatalysts for industrial exploitation.