Lipopolysaccharides (LPS) are amphipathic molecules that can self-aggregates into different sizes and structures.&lt;span style="font-size:10.8333px"&gt; &lt;/span&gt;LPS molecules are also an important pathogen that comes from the gram-negative bacteria external cell wall and triggers a signal within the innate immune system. To occur the LPS agonist role in humans, it is necessary to stimulate the toll-like receptor 4 (TLR4) by using its six acyl chain from its lipid A moiety. The effect of this LPS triggered signal includes an initial strong inflammatory response by the immune system that subsequently is counteracted via the human enzyme acyloxyacyl hydrolase (AOAH). In nature, AOAH detoxifies LPS by removing fatty acids from the lipid A component. The main purpose of this study is to mimic this biological response in-vitro by exploring additional enzymes in order to develop a sustainable water treatment technology. Removing LPS from water systems had been a challenge because of the high variability of their molecular weights. Furthermore, this molecule had shown relative stability to temperature and pH changes resulting in no structure change. In this study, we aim to explore a new detoxification mechanism with a catalytic de-acylation procedure using lipases. The product of the de-acylation reaction had been characterized via gas chromatography (GC), free fatty acid assays (FFA), dynamic light scattering (DLS), among others. Results have demonstrated the viability of the reaction that will serve as the groundwork principle to develop further technology for water purification. The details for this investigation methods and analytical techniques will be presented.<br/>

Investigating the in-vitro response of bacterial lipopolysaccharides de-acylation via enzymatically activated hydrolysis in water

ACS Fall 2020 Virtual Meeting

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