Abstract

The construction of enzyme mimics using protein protection layers possesses advantages of high biocompatibility and superior catalytic activity, which is desirable for biomedical applications including diseases diagnosis. Here, from E. coli expression system, recombinant protein of camel serum albumin (rCSA) from Camelus bactrianus was successfully obtained to encapsulate hemin via the self-assemble method without additional toxic organic reagents. As compared with that of horseradish peroxidase, the produced rCSA-hemin nanoparticles exhibited enhanced enzyme-mimicking activity and stability under harsh experimental conditions. Additionally, the steady-state kinetic analysis of rCSA-hemin in the solution revealed its higher affinity to the substrates. Therefore, a colorimetric detection method of H2O2 and glucose was constructed with a linear range of 2.5–500 μM with an LOD of 2.39 and 2.42 μM, respectively, which was also applied for the determination of glucose in the serum samples with satisfying recovery ratio ranging from 101.1% to 112.1%. The constructed camel protein-derived nanozyme system of remarkable stability holds promising potentials for the versatile biomedical uses.

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