Desolvation-induced formation of recombinant camel serum albumin-based nanocomposite for glutathione colorimetric determination

Protein-based enzyme mimics hold advantages of easy preparation, desirable compatibility and superior catalytic performance. Taking advantage of the remarkable stability of Bactrian camel serum albumin (CSA) compared with its counterpart in human and bovine, here a novel hemin-loaded nanozyme system was prepared through the desolvation method using a recombinant CSA (rCSA). The obtained hemin-rCSA nanoparticles exhibited improved enzyme mimic activity with higher affinity to the substrates compared with bare hemin and horseradish peroxidase. Moreover, the particle size and morphology of hemin-rCSA NPs was adjustable by the optimization of ethanol addition during the desolvation process. With the efficient encapsulation of hemin in the protein nanocomposite, a colorimetric detection of glutathione with the linear calibration concentration range of 3.2-100 mu M with an LOD of 0.667 mu M was achieved within 8 min. The available camel-derived serum albumin of recombinant form of improved stability provides a robust and manipulable protein-based nanoplatform for the molecular design of nanozyme system with enormous biomedical potentials.

Automated summary

Protein-based enzyme mimics have advantages of easy preparation, compatibility, and superior catalytic performance. A novel hemin-loaded nanozyme system was prepared using a stable Bactrian camel serum albumin. The obtained nanoparticles showed improved enzyme mimic activity and higher affinity to substrates, with adjustable particle size and morphology.