Influence of nanoencapsulated lutein on acetylcholinesterase activity: In vitro determination, kinetic parameters, and in silico docking simulations

Lutein is a bioactive found in dark leafy vegetables that may be used as a nutraceutical agent in foodstuff and an inhibitor of key enzymes of the human body such as those involved in the cholinergic system. However, its high hydrophobicity leads to low bioavailability and must be overcome if lutein is to be added in foods. The objective of this study was to evaluate the influence of nanoencapsulated lutein in the activity of the acetylcholinesterase enzyme. The in vitro study was carried out using water in order to evaluate the impact of encapsulation on the hydrophilicity of lutein. In vitro assays showed that lutein, both free and nanoencapsulated, presented a mixedtype inhibition behavior, and encapsulated lutein was able to inhibit acetylcholinesterase activity even in an aqueous medium. Inhibition was also showed by the in silico docking results which show that lutein interacted with the pocket region of the enzyme.info:eu-repo/semantics/publishedVersio

Bioactive evaluation and application of different formulations of the natural colorant curcumin (E100) in a hydrophilic matrix (yogurt)

Curcumin (E100) is a natural colorant that, besides conferring color, has bioactivity, serving as an alternative to some artificial colorants. As a hydrophobic colorant, its modification/compatibilization with the aqueous medium is required to improve stability and enable its application in hydrophilic food matrices. Herein, different formulations of curcumin (curcumin powder: PC, water-dispersible curcumin: DC: and nanoencapsulated curcumin: NC) were evaluated as yogurt colorants. PC showed the strongest bioactivity in all assays (EC50 values: 63±2 to 7.9±0.1 μg.mL-1; GI50 values: 48±1 to 17±1 μg.mL-1 and MIC values: 0.0625 to 0.5 mg.mL-1), which might indicate that DC and NC reduce the short-term accessibility to curcumin. The tested curcumin formulations produced yogurts with different appearance, specifically associated with their color parameters, besides presenting slight changes in nutritional composition and free sugars and fatty acids profiles. The water compatible formulations (DC and NC) showed advantages over hydrophobic (PC) having a wider industrial utilization.info:eu-repo/semantics/publishedVersio

Influence of ohmic heating on lentil protein structure and protein-pectin interactions

Proteins are essential for creating structured food systems due to their interactions with other molecules, but their structure is highly affected by temperature. This study aimed to evaluate the effects of different thermal processes (conventional and ohmic heating) on lentil protein structure and its interactions with pectin. The results showed that thermal processes can modify lentil protein structure, with the extent of modifications depending on the treatment temperature, electric field strength, and pH of the protein fraction extraction. Lentil protein extracted at pH9 was more stable to temperature variation under ohmic heating. When a low electric field strength (5V/cm) was applied, there was an increase in the hydrophobic surface and accessibility of sulfhydryl groups. In contrast, lentil protein extracted at pH7 was highly affected by all thermal treatments. Although structural changes were observed in some protein features, no influence was identified regarding lentil protein-pectin interactions. In conclusion, ohmic heating treatment has the potential to modify lentil protein structure, but the outcomes may depend on the extraction method used, which can dictate different structural arrangements of the native protein fraction. Industrial relevance The development of plant-based products have increased in the last years and other proteins, instead of soybean and pea, are required to meet new consumers' needs. Lentil protein is a non-soy, gluten free, and plant-based protein that could be an alternative to the plant-based market. These proteins can act as texturizing, emulsifying, foaming, and gelling agents but their suitable performance is dependent on protein structure. Thermal processes are a necessary component of food production, requiring careful control of the conditions involved as heat can drastically modify the structure of proteins, Therefore, in this study, the effects of two thermal processes (conventional and ohmic heating) on lentil protein structure and its interactions with pectin were evaluated. These findings may provide insights for developing more appropriate processes to preserve protein structure during food processing at industry.The authors are grateful to the São Paulo Research Foundation (FAPESP, processes #18/21987-1, #18/16456-7, #19/18704-0) and National Council for Scientific and Technological Development (CNPq, process # 309326/2022-2) for providing funding for this research.info:eu-repo/semantics/publishedVersio