Nanozyme can substitute a natural Ogataea polymorpha catalase enzyme in vivo

Nanomaterials possessing artificial, enzyme-like catalytic activity (nanozymes, NZs) have a great potential for application in research, immunological assays, biosensors, in vivo imaging, and as therapeutic agents. Despite the obvious advances in construction and understanding of functional properties of NZs, there is still no clear evidence of whether they can complement the loss of corresponding enzymatic activity in vivo. Herein, we report the first, to the best to our knowledge, example of successful substitution of natural enzyme activity by catalase-like platinum (nPt) and platinum-gold (nPtAu) nanoparticles transferred to the cells of methylotrophic yeast Ogataea polymorpha. The nPt NZs were synthesized by the chemical reduction method and used as a seed to produce the nPt(core)Au(shell) particles. The produced nPt NZs were 68.1 and 91.3 nm in size, while the hydrids were of 531.2 and 615.1 nm. Both nPt and nPtAu demonstrated catalase activity in vitro. The catalase-deficient strain Ogataea polymorpha C-105 was shown to be able to grow on methanol and a mixture of glucose and methanol in the presence although not in the absence of NZs, this correlating with the decrease in intracellular hydrogen peroxide production. The results provide the first example of complementation of the natural enzyme function by synthetic NZs, the phenomenon which can further be used in a screening for new catalase-like nanozymes and as a fruitful tool to modify living cells by nanoparticles possessing catalytic activity and to use such modified cells as sensitive elements in cell-based biosensors. Graphical abstract