Structure-Based Modeling of the Mechanical Behavior of Cross-Linked Enzyme Crystals

Because of their high volumetric catalytic activity, in addition to chemical and thermal resistances, enzymes the form protein crystals are an excellent choice for application as immobilized biocatalysts. However, mechanical stability is a requirement processability immobilisates, retaining enzymatic this closely related crystal structure. In study, influence engineering on cross-linked enzyme (CLECs) was investigated using genetically modified model which additionally cysteines were introduced surface targeted cross-linking. The results showed that mutant proteins native decreased compared wild-type crystals. specific cross-linking amino acid residues resulted increased CLECs. order determine correlation between structure resulting properties CLECs enable cross-linking, previously developed revised then used two proteins. This can explain mechanically relationships, such anisotropic behavior linker or mutation micromechanical and, hence, be helpful tailor-made production