Stepwise Thermophotochemical Crosslinking for Enzyme Stabilization and Immobilization

Abstract

Non-covalent bonding (e.g. electrostatic or ionic, hydrophobic and hydrogen bonding) is very important in maintaining the intra- and intermolecular interactions critical to the functioning of biological macromolecules in aqueous environments. The three-dimensional structure compatible with these functional interactions is stabilized in most enzymes by covalent non-peptide (e.g. disulfide) bonds. The introduction of additional covalent bonds within and between enzyme molecules thus seems to be a reasonable approach to the stabilization of the functional interactions for their subsequent study and use in unnatural environments.