A proteolytic nanobiocatalyst with built-in disulphide reducing properties

We report a method to equip proteolytic nanobiocatalysts with intrinsic disulphide bond reducing properties. After immobilisation onto silica particles, selected protease enzymes are partially shielded in a nanometre-thick mercaptosilica layer acting not only as a protective system but also as a substrate reducing agent. The biocatalysts produced efficiently perform simultaneous disulphide bond reduction and protein digestion. Besides a significant simplification of the proteolysis process, this strategy allows for a drastic increase of the enzyme stability.

Automated summary

This method equips proteolytic nanobiocatalysts with intrinsic disulphide bond reducing properties by immobilizing selected protease enzymes onto silica particles and forming a nanometre-thick mercaptosilica layer, allowing efficient simultaneous disulphide bond reduction and protein digestion, leading to a significant increase in enzyme stability while simplifying the proteolysis process.