We combine structural analysis, biochemical characterization, and protein engineering to understand how active-site architecture, substrate recognition, and cofactor binding control catalysis. These insights guide the design of enzymes with altered specificity, activity, stability, and cofactor preference.
We engineer Saccharomyces cerevisiae, Yarrowia lipolytica, and Pichia pastoris as complementary eukaryotic chassis. By combining metabolic engineering, protein secretion, genome engineering, and synthetic biology, we develop strains for high-value biochemicals, recombinant proteins and enzymes, and the discovery and validation of biological parts.
We investigate biological carbon-condensation and chain-building systems that convert simple precursors into larger and more complex molecules. Our work spans reverse β-oxidation, fatty acid synthases (FASs), polyketide synthases (PKSs), nonribosomal peptide synthetases (NRPSs), and engineered pathways for bioplastic monomers and polymers.
We study large multi-domain enzyme systems, including modular polyketide synthases, as programmable biosynthetic assembly lines. Our work examines module boundaries, inter-domain recognition, substrate transfer, and structure-guided mutagenesis to redesign their product-forming logic.
We investigate meroterpenoids as hybrid molecules formed by coupling terpene units with chemically diverse non-terpenoid partners, including polyketide-, shikimate-, alkaloid-, and other biosynthetic scaffolds. We study the prenyltransferases, cyclases, and tailoring enzymes that assemble and diversify these complex natural products.
We study the enzymes, fungi, yeasts, lactic acid bacteria, and metabolite changes that shape nuruk-based Korean alcoholic fermentation. This work links enzyme-mediated saccharification and microbial succession to alcohol production, flavor, and product quality.