Systematic Optimization of Interface Interactions Increases the Thermostability of a Multimeric Enzyme

摘要

With their exceptional selectivity, biocatalysts play an increasing role in diverse chemical fields including food processing, production of fine, specialty, and bulk chemicals, and fuel production. A frequently remaining fundamental limitation is operational stability, in particular at higher reaction temperatures, which are often preferred because of an increase in reaction rate or reactant solubility, a decrease in medium viscosity or risk of microbial contamination, or a more favorable position of the reaction equilibrium. However, the structural integrity of an enzyme, especially of mesophilic origin, is often impaired under these high-temperature operational regimes. Inactivation typically starts with a loss of integrity of the quaternary (for multimeric enzymes) or tertiary structure (for monomeric enzymes) and is followed by an irreversible denaturation step.