BUSCADOR RECOLECTA

Excel file including: - the degree of hydrolysis, antioxidant activity evaluated by DPPH, FRAP and ABTS assays, peptide separation by reverse phase chromatography (RP-HPLC), peptide identification by mass spectrometry in tandem, peptides antioxidant activity and IC50 calculation., As major industrial poultry by-products, chicken feet are considered as notable sources of several bioactive molecules. The current work covers the processing of chicken feet proteins as substrates to be hydrolysed by combinations of three commercial enzymes (Alcalase®, Flavourzyme® and Protana® Prime) during different hydrolysis periods and the evaluation of the identified peptides having antioxidant activity after simulated gastrointestinal digestion., Grant PID2020-119684RB-I00 funded by MCIN/AEI/10.13039/501100011033 is acknowledged. Dr. Ozturk-Kerimoglu gratefully acknowledges the financial support of the Scientific and Technological Research Council of Türkiye (TÜBİTAK) Science Fellowships and Grant Programs Directorate within the Post-Doctoral Fellowship 2219 Program., 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

With the institutional support of the ‘Severo Ochoa Centre of Excellence’ accreditation (CEX2019-000928-S)., No

Sanger sequencing results from the CASR gene analysis in the F2 generation CaSR_F2., Peer reviewed

Excel file including: Proximate composition and physicochemical parameters of porcine organs, antioxidant activity of pork organs (ABTS, DPPH and FRAP), total nucleotides (mg nucleotide/100g organ), free amino acids (mg amino acid/g organ), and total amino acids (mg amino acid/g organ)., The increase in world population has generated a higher demand for quality proteins, increasing the production in meat industry but also the generation of thousands of tons of by-products, with a negative economic and environmental impact. The valorisation of slaughterhouse by-products by giving by-products a new use as food ingredient is one of the best strategies to add value while reducing environmental damage. Flavour is one of the most influential parameters in the purchasing decision of consumers, and in meat products it is mostly influenced by the content in free amino acids and nucleotides. In this study, the potential of 4 pork organs (liver, kidney, lung, and brain) as a source of flavour-related substances was investigated. Liver proved to be the organ showing the highest content of free and total amino acids related to taste, while kidney was the organ with the highest content of umami nucleotides. The results of the Taste Activity Value indicated that umami, sweet, and bittersweet amino acids are main responsible for the taste of the organs. On the other hand, the synergy between amino acids and nucleotides in relation with umami taste was determined, showing liver and kidney the best values in Equivalent Umami Content. In addition, the antioxidant activity of the organs was determined, and liver and kidney showed the highest antioxidant activity in all assays (p < 0.05). In conclusion, pork organs, especially liver and kidney, may be good candidates to be used as raw materials to produce functional flavouring ingredients., This work was supported by the Project PID2020-119684RB-I00 and grant PRE2021-100576 to MILM funded by MCIN/ AEI /10.13039/501100011033 and European Social Fund are acknowledged. The Accreditation as Center of Excellence Severo Ochoa CEX2021-001189-S funded by MCIN/AEI / 10.13039/501100011033 is also fully acknowledged, With funding from the Spanish government through the ‘Severo Ochoa Centre of Excellence’ accreditation (CEX2021-001189-S), Peer reviewed

5 figures, 1 table.-- Under a Creative Commons License BY NC ND 4.0, https://creativecommons.org/licenses/by-nc-nd/4.0/., Fig. S1. Temperature profile along the reactor at 500 ºC. Left: at 6 kg/h; right: at 9 kg/h. Fig. S2. TG and DTG curves of PS. Fig. S3. Some images of the operational issues related to feed screw blockages and polystyrene blocks formation. Fig. S4. Volatile residence time variation as a function of PS feeding rate. Fig. S5. Spectrum analysis GC. Table S1. GC/MS analysis. Volatiles residence time estimation: To calculate the residence time of volatiles released during the pyrolysis of PS (polystyrene), various parameters need to be considered. These include the volume available for the feedstock in the auger, which depends on the auger diameter and the design of the auger pitch, as well as different process parameters such as the feed rate and the density of volatiles., Peer reviewed

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

Esta publicación es parte del proyecto de I+D+i Escritores latinoamericanos en los países socialistas europeos durante la Guerra Fría (PID2020-113994GB-I00), financiado por MCIN/ AEI/10.13039/501100011033/., Recopilación hemerográfica de textos relativos a la literatura latinoamericana. Para más detalles, véase el fichero Readme adjunto. Material procedente de la biblioteca de la Universidad del Oeste de Timisoara: https://bcut.ro/ Collection of periodicals on Latin American literature. For more details, see the attached Readme file. Material from the Library of the West University of Timisoara: https://bcut.ro/, Esta publicación es parte del proyecto de I+D+i Escritores latinoamericanos en los países socialistas europeos durante la Guerra Fría (PID2020-113994GB-I00), financiado por MCIN/ AEI/10.13039/501100011033/., No