BUSCADOR RECOLECTA

The representation of PCoA in RGB space as showed in the Atlas (a) and the resulting haplotype map (b) for 36 specimens of Limenitis lorquini., Peer reviewed

Haplotype maps for 36 specimens of Limenitis lorquini (a) and 102 specimens of Limenitis arthemis (b)., Peer reviewed

PCoA (a) and haplotype network (b) for 36 specimens of Limenitis lorquini. Because colors assigned to haplotypes are the same for the PCoA and the haplotype network, it is possible to easily identify same haplotypes in the two plots., Peer reviewed

Values for all species in the Atlas are depicted as grey bubbles and the species of interest (Limenitis lorquini) is represented by a purple dot. The black lines represent median values for all species of the Atlas., Peer reviewed

MMC S1. The optimization process of the RFCN structure and hyperparamters in FT_RFCN are illustrated in detail., Peer reviewed

The dataset consist of one file with contains measurement data from the weather station of the MAGIC telescope from the year 2003 until 2023. Due to the long series of measurements, various quality assurance measures were carried out, such as removing obviously incorrect values from an individual measurement sensor. The format of the file is HDF5 and contains various columns as described by the metadata file., Peer reviewed

No

Excel file including: Degree of hydrolysis, the inhibition of DPP-IV of 5 enzymatic hydrolysates of chicken blood, peptide separation of 2 hydrolysates by reverse phase chromatography (RP-HPLC); assay of DPP IV activity and free amino acids composition per fraction, peptide identification by mass spectrometry in tandem, in silico analysis and DPP IV inhibitory activity for each synthetised peptide., Blood is a meat by-product rich in proteins with properties that can be improved after hydrolysis, making it a sustainable alternative for use in the generation of bioactive peptides. The objective of this study was to identify dipeptidyl peptidase IV (DPP-IV) inhibitory peptides obtained from different chicken blood hydrolysates prepared using combinations of four different enzymes. Best results were observed for AP (2% Alcalase + 5% Protana Prime) and APP (2% Alcalase + 5% Protana Prime + 3% Protana UBoost) hydrolysates obtaining inhibition values of 60.55 and 53.61%, respectively, assayed at a concentration of 10 mg/mL. Free amino acids were determined to establish the impact of exopeptidase activity in the samples. A total of 79 and 12 sequences of peptides were identified by liquid chromatography and mass spectrometry in tandem (LC-MS/MS) in AP and APP samples, respectively. Nine of the identified peptides were established as potential DPP-IV inhibitory using in silico approaches and later synthesized for confirmation. Thus, peptides GPF, IGL, and GGGW showed good DPP-IV inhibitory activity with IC50 values of 0.94, 2.22, and 2.73 mM, respectively. This study confirmed the potential of peptides obtained from chicken blood hydrolysates to be used as DPP-IV inhibitors and, therefore, in the control or modulation of type 2 diabetes., Grant PID2020-119684RB-I00 funded by MCIN/AEI/10.13039/501100011033. Grant GRISOLIAP/2020/021 de la Consellería de Innovació, Universitats, Ciència I Societat Digital de la Generalitat Valenciana (GCA) is also acknowledged., Peer reviewed

Excel file including: Degree of hydrolysis (DH), free amino acid content, antioxidant activity (DPPH, FRAP and ABTS assays) and inhibition of dipeptidyl peptidase IV (DPP-IV), angiotensin-converting enzyme (ACE-I) and neprilysin enzyme (NEP), from Spanish dry-cured ham bone samples, with and without heat treatment and subsequently hydrolyzed with four different enzymes (Protamex, Flavourzyme, Protana prime and Alcalase), in addition to a control sample (without hydrolysis). Also the molecular weight distribution of peptides in the hydrolyzates. The hydrolyzates that were heated prior to hydrolysis were also subjected to in vitro gastrointestinal digestion and subsequently all of the above variables were re-evaluated to determine the stability of the bioactive peptides contained in the ham bone hydrolyzates to gastrointestinal digestion (GI-D)., This study reports the effect of thermal pretreatment and the use of different commercial proteolytic enzymes (Protamex, Flavourzyme, Protana prime, and Alcalase) on the free amino acid content (FAA), peptide profile, and antioxidant, antidiabetic, antihypertensive, and anti-inflammatory potential (DPPH, FRAP, and ABTS assay, DPP-IV, ACE-I, and NEP inhibitory activities) of dry-cured ham bone hydrolyzates. The effect of in vitro digestion was also determined. Thermal pretreatment significantly increased the degree of hydrolysis, the FAA, and the DPP-IV and ACE-I inhibitory activities. The type of peptidase used was the most significant factor influencing antioxidant activity and neprilysin inhibitory activity. Protana prime hydrolyzates failed to inhibit DPP-IV and neprilysin enzymes and had low values of ACE-I inhibitory activity. After in vitro digestion, bioactivities kept constant in most cases or even increased in ACE-I inhibitory activity. Therefore, hydrolyzates from dry-cured ham bones could serve as a potential source of functional food ingredients for health benefits., Grant PID2020-119684RB-I00 funded by MCIN/ AEI /10.13039/501100011033 is acknowledged. Grant GRISOLIAP/2020/021 de la Consellería de Innovació, Universitats, Ciència i Societat Digital de la Generalitat Valenciana (G.C.-A.) is also acknowledged. The accreditation as Center of Excellence Severo Ochoa CEX2021-001189-S funded by MCIN/ AEI /10.13039/501100011033 is acknowledged, With funding from the Spanish government through the ‘Severo Ochoa Centre of Excellence’ accreditation (CEX2021-001189-S), Peer reviewed

S1. Literature review classifications. S2. Additional figures. S3. Tables., Peer reviewed