Study on hydrolase mechanism of copper compound nanoparticles and its application in the evaluation of gut bacteria in aquatic environment

Conversing proteinaceous enzyme behavior into nanomaterials is intriguing academically, but the threshold from mimicry to accessing sophisticated biological entities has not yet been crossed. Herein, we disclosed the pan-glycoside hydrolases-like (p-GHs-like) activities of Cu3P and Cu2O nanoparticles and decently confirmed their consistent catalytic mechanism as natural glycoside hydrolase, that is, the precise bond breaking, anomeric carbon configuration and catalytic attack mode. We then introduced p-GHs-like NPs into Escherichia coli to establish a feedback regulatory model for the β-D-glucuronidase (expressed by uidA) that was initially expressed in trace amounts. An upregulation of uidA from 72 to 1000 counts was induced by the p-GHs-like activities via pre-released β-glucuronides derivatives, further contributing to 1–2 orders enhancement of the enzyme production. We unearthed the specific catalytic mechanism to unlock a black box of enzyme-like inorganic feedback on the natural enzyme synthesis process, pushing mimicry leaped to physiological behavior.