Acrylamide increases and furanoic compounds decrease in plant-based meat alternatives during pan-frying.

Plant-based meat alternatives are gaining popularity as protein sources. However, pan-frying may lead to the formation of potentially harmful food contaminants. We investigated the formation of acrylamide and furanoic compounds in four different plant-based meat alternatives and two meat burger patties during pan-frying at 160 and 200 °C. The highest acrylamide contents (72. ± 7.7 and 69.2 ± 9.5 µg/kg, respectively) were found in soy flour- and sunflower-protein based patties fried at 200 °C. Unprepared pea and soy protein-based burger patties contained the highest furfural amounts (2832.8 ± 576.2 and 2683.0 ± 868.5 µg/kg, respectively). Furfuryl alcohol content was highest in soy flour-based patties and increased temperature-dependently up to 1120.9 ± 383.4 µg/kg. Based on the tolerable intake calculated by the EFSA Scientific Panel on Contaminants in the Food Chain, these amounts do not pose a health risk. Nevertheless, since plant-based novel food are being increasingly consumed, further investigations into the formation of food contaminants in novel processed foods are warranted.

Prumnopitys Andina Fruit Extract Activates Liver X Receptors after In Vitro Digestion.

SCOPE: 20-Hydroxyecdysone (20E) is the main phytochemical present in the fresh arils of Prumnopitys andina. 20E is reported to have anabolic effects by modulation of gene transcription by interaction with nuclear receptors. Our aim is to evaluate the in vitro bioaccessibility, transepithelial transport of 20E, and the capacity of P. andina fruit extract and 20E to activate selected mammalian nuclear receptors in transiently transfected human cells after simulated gastrointestinal digestion. RESULTS: 20E shows good stability, solubility, and micellization after in vitro digestion. 20E is taken up by Caco-2 cells, but poorly transported through the epithelial cell membrane, possibly due to P-glycoprotein-mediated efflux. In transiently transfected HepG2 cells, the fruit extract significantly induces the signal intensity for the liver X receptor (LXR)-α and -ß by 1.6 and 1.4-fold, respectively. In contrast, the treatment with 20E, irrespective of its concentration, did not change the activity of both LXR receptors. No effects are observed for the pregnane X receptor or the constitutive androstane receptor. CONCLUSION: Our findings show that components of the digested P. andina extract other than 20E are responsible for the effects on LXR-α and -ß. Our findings open new perspectives on the potential role of P. andina fruits in cholesterol metabolism and inflammatory diseases.

Distinct Cell Types With the Bitter Receptor Tas2r126 in Different Compartments of the Stomach.

Cells expressing bitter taste receptors (T2Rs or Tas2rs) in extraoral tissues are considered to be chemosensory cells mediating protective responses to potentially harmful or even antiinflammatory or antimicrobial compounds. In a previous study the activity of the Tas2R143/Tas2R135/Tas2r126 cluster promoter in the stomach was monitored using a Cre-reporter mouse line. Reporter gene expression and Tas2r126 mRNA were found in brush cells located at the distal wall of the gastric groove. In this study, we explored whether brush cells and epithelial cells of the stomach in fact contain the Tas2r126 receptor protein. Using immunohistochemistry, we demonstrate the presence of Tas2r126 immunoreactivity in different cell populations in the glandular stomach, in a subset of brush cells at the gastric groove and in unique glandular units as well as in certain enteroendocrine cells. In brush cells at the gastric groove, a strong immunofluorescence signal for the Tas2r126 receptor was observed at the most apical region of the cells, i.e., the microvillar tuft. In addition, we found a high density of Tas2r126-positive brush cells in the unique glandular units. These invaginations are located distally to the groove, open directly into the furrow and are enwrapped by smoothelin-immunoreactive muscles. In the corpus, Tas2r126 immunoreactivity was found in histamine-producing ECL cells and in ghrelin-producing X/A-like cells, the main enteroendcrine cells of this compartment. In the antrum, Tas2r126 labeling was observed in serotonin-storing EC cells and ghrelin cells, both representing only minor populations of enteroendocrine cells in this compartment. In conclusion, our data provide evidence for the presence of the Tas2r126 receptor protein in distinct cell types in the epithelium lining the mouse stomach which render the stomach responsive to agonists for bitter receptors.