The Depth-Dependent Mechanical Behavior of Anisotropic Native and Cross-Linked HheG Enzyme Crystals

Enzymes are able to catalyze various specific reactions under mild conditions and can, therefore, be applied in industrial processes. To ensure process profitability, the enzymes must reusable while ensuring their enzymatic activity. improve processability immobilization of biocatalyst, can be, e.g., crystallized, resulting crystals cross-linked. These mechanically stable catalytically active particles called CLECs (cross-linked enzyme crystals). In this study, influence cross-linking on mechanical catalytic properties halohydrin dehalogenase (HheG) was investigated using nanoindentation technique. Considering viscoelastic behavior protein crystals, a investigation performed at different indentation rates. addition hardness, for first time, depth-dependent fractions elastic plastic deformation energies were determined crystals. The results showed that hardness HheG indentation-rate-insensitive decrease with increases penetration depth. Our fraction energy indicated anisotropic crystal higher irreversible prismatic faces. Due cross-linking, faces increased from 8% basal 68% This study demonstrates enhanced have good activity are, suitable use.