Seoul National University · Engineering
Professor Yoon-Mo Koo's research lab specializes in biocatalysis and sustainable chemical processes, with a focus on enzyme-mediated synthesis of high-value biobased products such as sugar fatty acid esters and rare sugars. The lab integrates experimental studies with molecular dynamics simulations to understand and optimize enzyme behavior in non-aqueous environments like ionic liquids and organic solvents. Key research directions include enhancing the efficiency and scalability of lipase-catalyzed reactions, developing novel solvent systems for improved substrate solubility, and applying advanced separation techniques such as simulated moving bed (SMB) chromatography for product purification. The lab also investigates the economic and environmental feasibility of carbon capture and storage technologies, particularly in industrial sectors like steel production.
Figures are computed from collected data and may differ slightly.
This study examines the environmental impacts of roundtrip car sharing services by investigating transportation behavior. Car sharing should contribute to reduced greenhouse gas GHG emissions; however, such schemes include both positive and negative environmental effects, including: (1) reduced CO2e (carbon dioxide equivalent) from substituting private vehicle use for more fuel-efficient car sharing vehicles, (2) increased CO2e as car-less individuals switch from public transit to car sharing ve
The low solubility of sugars has hampered the lipase-catalyzed synthesis of fatty acid sugar esters in organic solvents and ionic liquids (ILs), because several solvents that are able to effectively dissolve sugars are detrimental to enzymes. In this work, in order to prepare a high concentration of sugars in ILs, we have developed a new procedure that entails mixing an aqueous sugar solution into ILs followed by removal of the water from the solution. The glucose concentrations in the supersatu
Candida antarctica lipase B (CALB) is an efficient biocatalyst for hydrolysis, esterification, and polymerization reactions. In order to understand how to control enzyme activity and stability we performed a combined experimental and molecular dynamics simulation study of CALB in organic solvents and ionic liquids (ILs). Our results demonstrate that the conformational changes of the active site cavity are directly related to enzyme activity and decrease in the following order: [Bmim][TfO] > tert
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