Cu2O/SBA-3 Possess Intrinsic High Protease-Like Activity for Efficient Hydrolysis of Protein Under Physiological Conditions

Developing efficient artificial proteases still remains a great challenge due to the high stability of peptide bonds. Nanozymes have attracted great attention for their high stability, low cost and inherent physicochemical properties, providing new opportunities to break through natural enzyme inherent limitations, but the intrinsic mimic proteases properties of nanomaterials were seldom explored. Herein, we describe for the first time that SBA-3 supported Cu2O (Cu2O/SBA-3) exhibited excellent protease-like activity to hydrolysis of bovine serum albumin (BSA) and casein under neutral conditions, which is even superior to natural proteases (trypsin) and most of the other protease mimics under identical conditions. It exhibited surprisingly high catalytic activity and possessed good stability. As the first example of protease mimics consist of metallic compounds and mesoporous materials, Cu2O/SBA-3 has many advantages, such as easy preparation and separation, high activity and stability, mild reaction conditions, which makes this catalytic system have multiple of potential applications in biological systems.

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