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Recently enzymes have been taking on increasingly crucial and substantial roles in both industrial and household applications. These enzymes are often expensive and easily denatured in the presence of extreme environments. In this study we explored the enzymatic capabilities of a synthetic functional molecule attached to various polymer supports which could be capable of overcoming the obstacles faced by traditional enzymes. This strategy allows the attachments of the catalytic triad – three amino acid residues known to form a complex catalytic mechanism to degrade esters and amide bonds. Furthermore, enzyme-like binding sites can be designed by controlling the hydrophobicity of the polymeric backbones. After attaching a triad-functionalized molecule consisting of an acid, imidazole, and hydroxyl functional groups to various polymeric platforms using the Azide-Alkyne Huisgen Cycloaddition reaction, we employed UV spectroscopy to monitor the real-time breakdown of assorted lipid substrates under exposure to these polymers. We discovered varying levels of enzymatic capabilities which followed interesting and unexpected trends related to the hydrophobicity of both the substrate and polymer. The most promising candidate for a synthetic enzyme is a recyclable, cross-linked resin which rivals the enzymatic potential of lipase under certain reaction conditions. The process of developing a working synthetic enzyme with a triad of functional groups has never been successfully attempted before. The result of this study, whereby the hugely-complex nature of an important enzyme can be replicated, is a significant breakthrough into an uncharted field of polymer chemistry.