Isolation and characterization of lipase inhibitory activity from Solanum tuberosum L

Abstract

Previous studies using 14 different cultivars of Solanum tuberosum L.showed that patatins, lipid acyl enzymes, have varied activities and are regulated by lipase inhibitory compound. In this study we isolated the lipase inhibitory compound by serial solvent extraction and using several chromatographic methods. The inhibitory compound showed high solubility in water and weak solubility in butanol and ethyl acetate. This solubility property suggests that the molecule may have both hydrophilic and hydrophobic moieties. Inhibition kinetics study showed that the compound may have mixed type inhibition as it may interact with the substrate and is markedly influenced by the structure of ester bond or lipid emulsion. The compound also exhibited high potency with an estimated IC50 of 216 ng/mL in the impure extract. The potency of the lipase inhibition of the compound is comparable to the commercially available anti‐obesity drug, Orlistat, whose LC50 was 0.4 ng/mL. Taken together with stability of the inhibitory compound during storage, high temperature and low pH stability, it presents many possibilities in developing applications in anti‐obesity remedies with less likelihood of side‐effects related with hydrophilic lipase inhibitors currently in use in the global market.Support or Funding InformationKorea National Research FundThis abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.