In order to augment the cells with non-native functionality, proteins were conjugated to the clickable polymers using enzymes that were modified with a cycloalkyne linker. We selected the enzyme β-galactosidase (β-gal), as it is not expressed by S. cerevisiae. The post-hoc conjugation of βgal-DBCO proved to be ineffective, possibly hindered by the PEG brushes (SI Figure ). We thus conjugated the macromonomer to the enzyme before polymerization, which brought the conjugation efficiency to 33% of the starting enzyme amount (Figure was β-gal able to yield the coloured o-nitrophenol from a chromogenic substrate (Figure ), but it could also increase the proliferation of yeast on lactose as the main carbon source (Figure ) -which it would otherwise not be able to metabolize-and improve the survival against the detergent octylglucopyranoside (Figure ), as it degraded this compound. To prove the versatility of the approach to functionalize cell surfaces with polymer-enzyme conjugates, alkaline phosphatase (ALP), an enzyme that is also not excreted by the yeast, was linked to the clickable monomer, which was then polymerized on the cells (SI Figure ). ALP too made the decorated cells produce onitrophenol; furthermore, the enzyme was able to induce the precipitation of calcium phosphate by cleaving the substrate calcium glycerophosphate, resulting in mineral clusters depositing around the cells, thus creating a novel mechanism for biomineralization mediated by S. cerevisiae (SI Figure ). Concluding, the experiments with two model enzymes show that self-synthesized polymer-enzyme conjugates can be used to install orthogonal catalytic activity onto yeast cells which strongly modifies the behaviour of the cells.