BUSCADOR RECOLECTA

Figure S1: Biplot-CATPCA using 'Duke' blueberry results of gene expression (XTH23, PL8, PG, PME3, EXP4, GH5), mechanical properties (MSBreaking, SlopeSB, DisplacementSB, SBWork), total decay, water loss (WLoss) and maturation index (MI) as variables. The component loadings of the variables are indicated by black lines, while the analyzed samples are represented by blue dots: [(1) freshly harvested; (2) 3 d Air, (3) 3 d 15% CO2, (4) 3 d 20% CO2, (5) 14 d Air, (6) 3 d 15% CO2 + 11 d Air, (7) 3 d 20% CO2 + 11 d Air, (8) 29 d Air, (9) 3 d 15% CO2 + 26 d Air, (10) 3 d 20% CO2 + 26 d Air]; Figure S2: Biplot-CATPCA using 'Ochlockonee' blueberry results of gene expression (XTH23, PL8, PG, PME3, EXP4, GH5), mechanical properties (MSBreaking, SlopeSB, DisplacementSB, SBWork), total decay, water loss (WLoss) and maturation index (MI) as variables. The component loadings of the variables are represented by black lines, and the analyzed samples are depicted by blue dots: [(1) freshly harvested; (2) 3 d Air, (3) 3 d 15% CO2, (4) 3 d 20% CO2, (5) 14 d Air, (6) 3 d 15% CO2 + 11 d Air, (7) 3 d 20% CO2 + 11 d Air, (8) 29 d Air, (9) 3 d 15% CO2 + 26 d Air, (10) 3 d 20% CO2 + 26 d Air]; Table S1: Primers used for the quantification of gene expression levels by RT-qPCR., Peer reviewed

Table S1: Tentative identification of one hundred and seven phenolic compounds in the different murta extracts., Peer reviewed

Table S1. Physicochemical, bioactive compounds, and antioxidant capacity of red beetroot powder. Table S2. Recipe for the formulation of beetroot dark chocolate. Table S3. Response optimization of beetroot dark chocolate PCA clusters based on nutritional composition, sugars, bioactive compounds, and antioxidant capacity, with overall composite desirability and contributions of the individual measured parameters., Peer reviewed

The dataset contains a list of polygons delineated on historical photographs (early 20th century) in the Ordesa and Monte Perdido National Park, characteristics asociated, land cover, and fate after about 100 years later (photographs were repeated between 2018-2021). Historical and new photographs are available at https://paisajescentenarios.csic.es, Peer reviewed

-Experimental procedures, characterization data, and copies of the NMR spectra. -FAIR Data is available as Supporting Information for Publication and includes the primary NMR FID files for compounds: [4C, 40, 4O-OBn, 4S, 4S-tBu, 8C, 8O, 8S, 10a, 10b, 10b-AA, 10c, 10d, 12a, 12b, 12c, 12c–OH, 12d, 12e, 14c, 14d]. See FID for Publication for additional information., Peer reviewed

NMR spectra, emission and excitation spectra, lifetime fitting curves, XRD spectra, crystal X-ray diagrams, bond distances and angles., Peer reviewed

-Miscellaneous information, including NMR data of complexes and organic products, and DFT calculation data (PDF). -Optimized coordinates for the computed compounds (XYZ)., Peer reviewed

Figure S1. Fold change in gene expression was measured 8 h after 25 or 50 μg/mL chicken TM, shrimp TM or OVA exposure in Caco-2 cells cocultured with PBMCs. mRNA expression of the alarmins (A) Il33, (B) Il25, and (C) Tslp was increased upon exposure to either concentration of sshrimp TM. D) LDH release and (E) WST conversion by Caco-2 cells and HT-29 cells respectively was not affected 48 h after exposure in 96 wells flat bottom plates to increasing doses of chicken TM, shrimp TM or OVA. (F) A multiplex array was performed on supernatants from Caco-2 cells and HT-29 cells that were exposed to 25 and 50 μg/mL chicken TM or shrimp TM, or 50 μg/mL OVA. Next to the increased secretion of IL25, TSLP, IL1β, CCL22, and TNFα after exposing HT-29 cells to 50 μg/mL sdhrimp TM, a similar effect on cytokine secretion was seen after exposure to 25 μg/mL shrimp TM. Both chicken TM exposures decreased secretion of IL1α in Caco-2 cells, but exposure to this low-allergenic protein did not induce any other changes in cytokines secretion from Caco-2 cells or HT-29 cells. Data is analyzed by One-Way ANOVA or Friedman test when data did not fit a normal distribution, n = 3 or n = 5, mean ± SEM (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001). Figure S2. HT-29 cells were exposed to increasing doses of chicken TM, shrimp TM or OVA for 48 h in 96 wells flat bottom plates. Secreted A) IL33, B) TSLP, C) IL8, D) CCL20, and E) CCL22 were measured by ELISA. Exposure to chicken TM did not enhance cytokine secretion, exposure to shrimp TM and OVA induced a dose-dependent enhanced secretion of IL8 and CCL20. Data is analyzed by One-Way ANOVA, n = 3, mean ± SEM (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001). Figure S3. After culture of moDC with or without HT-29 cells and coculture of primed DC with T cells, viability was assessed. Viability of A) HT-29 cells after 50 μg/mL shrimp TM exposure. B) Viability of moDC was not affected by chicken TM or shrimp TM exposure when cocultured with HT-29 cells. However when moDCs were directly exposed to TmH, cell viability was significantly decreased. Coculture of the primed DCs with T cells did not affect C) viability or D) IL10 secretion. E) Furthermore, the gating strategy used to determine the viable T helper cells population and corresponding FMOs are presented. Data is analyzed by One-Way ANOVA, n = 3, mean ± SEM (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001). Figure S4. A visual representation, using z-scores, of (A) the cytokine secretion from Caco-2 and HT29 cells cultured in 96 well flatbottom culture plates and, (B) cytokine secretion and marker expression upon exposure to chicken TM or shrimp TM in the IEC/DC/T cell coculture model. Figure S5. Amino acid (aa) sequence of recombinant chicken α-1 tropomyosin (UniProt P04268), including residual aa from cloning site (italic) and His6-Tag (bold), with a calculated molecular weight of 34.044 kDa and pI of 4.83 (Expasy ProtParam). Figure S6. Amino acid (aa) sequence of recombinant shrimp tropomyosin (UniProt A1KYZ2), including residual aa from cloning site (italic) and His6-Tag (bold), with a calculated molecular weight of 34.2 kDa and pI of 4.96 (Expasy ProtParam). Figure S7. (A) Coomassie-stained chicken tropomyosin after removal of endotoxin with a major protein band around 36 kDa. (B) Silver stained and Coomassie stained shrimp tropomyosin after removal of endotoxin with a major protein band around 35 kDa (M, molecular kDa marker; chTM, chicken tropomyosin; sTM, shrimp tropomyosin)., Peer reviewed

A Microsoft Excel workbook containing the Table S1: Antioxidant peptides with potential cleavage sites under in silico hydrolysis—bioactivity and bioavailability properties., Peer reviewed

MMC S1. Details calculation of elastic and thermal properties at different temperatures are given in the supplementary document., Peer reviewed