Peter Westh

EnZight identifies and prioritizes substitution hotspots in enzymes using structural alignment, demonstrating effectiveness in improving catalytic activity and thermostability.

The paper screens bacterial cutinases to identify those with PET hydrolysis activity, finding it rare and mostly within the canonical-fold family.

This study uses isothermal titration calorimetry to analyze the thermodynamics of CO2 capture by amino acids and peptides, revealing distinct optimization strategies for carbamate formation.

This study identifies and characterizes five novel bacterial urethanases capable of degrading polyurethanes, with u15 showing high catalytic efficiency and structural insights for biocatalytic recycling.

This study examines the relationship between substrate crystallinity, enzyme binding strength, and cellulase activity, revealing a linear free energy relationship with varying slopes linked to substrate crystallinity.

This paper develops a high-throughput screening pipeline to identify carbohydrate-binding modules (CBMs) that bind synthetic and natural polymers, discovering binders for PET, PE, PS, and polysaccharides, and demonstrating their utility in enhancing plastic-degrading enzyme activity.

The paper investigates how crystallinity affects enzymatic degradation of PET, finding that high crystallinity limits enzyme activity due to conformational constraints and reduces productive sites on the polymer surface.