Network Dynamics as Fingerprints of Thermostability in an In Silico-Engineered DyP-Type Peroxidase.

ABSTRACT: Stabilizing industrial enzymes is crucial for advancing environmentally responsible bioprocesses; however, the structural basis of thermostability remains incompletely understood. Here, we engineered thermostable variants of a tetrameric dye-decolorizing peroxidase (DyP) using two independent open-source design algorithms, yielding enzymes with significantly improved thermal performance and prolonged activity at elevated temperatures. Subsequent recombination strategies minimize the mutational burden while maintaining or enhancing stability. Structural and dynamic analyses of the thermostable variants revealed convergent features, including increased compactness, rigidity, and an enriched network of hydrogen bonds and hydrophobic interactions. Despite differing mutation profiles, stabilizi

SUBMITTER: Rodrigues CF 

PROVIDER: S-EPMC12418308 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature