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Resultados totales (Incluyendo duplicados): 31
Encontrada(s) 4 página(s)
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371374
Set de datos (Dataset). 2024

DATA OF MANUSCRIPT SEQUENTIAL ENZYMATIC HYDROLYSIS AND ULTRASOUND PRETREATMENT OF PORK LIVER FOR THE GENERATION OF BIOACTIVE AND TASTE-RELATED HYDROLYZATES

  • López-Martínez, Manuel Ignacio
  • Toldrá Vilardell, Fidel
  • Mora, Leticia
Excel file including: Conditions tested in the study, proximate composition and physicochemical parameters of porcine liver, degree of hydrolysis, antioxidant activity (ABTS, DPPH, FRAP and ORAC), ferrous ion chelating activity (% Chelation), and free amino acids (mg amino acid/g liver) of liver hydrolyzates., In the study of protein-rich byproducts, enzymatic hydrolysis stands as a prominent technique, generating bioactive peptides. Combining exo- and endopeptidases could enhance both biological and sensory properties. Ultrasound pretreatment is one of the most promising techniques for the optimization of enzymatic hydrolysis. This research aimed to create tasteful and biologically active pork liver hydrolyzates by using sequential hydrolysis with two types of enzymes and two types of ultrasound pretreatments. Sequential hydrolyzates exhibited a higher degree of hydrolysis than single ones. Protana Prime hydrolyzates yielded the largest amount of taste-related amino acids, enhancing sweet, bittersweet, and umami amino acids according to the Taste Activity Value (TAV). These hydrolyzates also displayed significantly higher antioxidant activity. Among sequential hydrolyzates, Flavourzyme and Protana Prime hydrolyzates pretreated with ultrasound showed the highest ferrous ion chelating activity. Overall, employing both Alcalase and Protana Prime on porcine livers pretreated with ultrasound proved to be highly effective in obtaining potentially tasteful and biologically active hydrolyzates., Grants PID2020−119684RB-I00 funded by MCINU/AEI/10.13039/501100011033 and PRE2021−100576 allocated to MILM, funded by MCIU/AEI/10.13039/501100011033 in conjunction with the European Social Fund, are acknowledged. The accreditation as Centre of Excellence Severo Ochoa CEX2021−001189-S, funded by MCIU/AEI/10.13039/501100011033, is also acknowledged., With funding from the Spanish government through the ‘Severo Ochoa Centre of Excellence’ accreditation (CEX2021-001189-S), Peer reviewed

DOI: http://hdl.handle.net/10261/371374, https://doi.org/10.20350/digitalCSIC/16643
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371374
HANDLE: http://hdl.handle.net/10261/371374, https://doi.org/10.20350/digitalCSIC/16643
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371374
PMID: http://hdl.handle.net/10261/371374, https://doi.org/10.20350/digitalCSIC/16643
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371374
Ver en: http://hdl.handle.net/10261/371374, https://doi.org/10.20350/digitalCSIC/16643
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371374

DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371527
Set de datos (Dataset). 2024

DATA OF MANUSCRIPT ANTIOXIDANT PEPTIDES GENERATED FROM CHICKEN FEET PROTEIN HYDROLYSATES

  • Ozturk-Kerimoglu, Burcu
  • Heres, Alejandro
  • Mora, Leticia
  • Toldrá Vilardell, Fidel
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

DOI: http://hdl.handle.net/10261/371527
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371527
HANDLE: http://hdl.handle.net/10261/371527
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371527
PMID: http://hdl.handle.net/10261/371527
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371527
Ver en: http://hdl.handle.net/10261/371527
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371527

DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371528
Set de datos (Dataset). 2024

DATA OF MANUSCRIPT POTENTIAL OF DRY-CURED HAM BONES AS A SUSTAINABLE SOURCE TO OBTAIN ANTIOXIDANT AND DPP-IV INHIBITORY EXTRACTS

  • Carrera Alvarado, Gisela
  • Toldrá Vilardell, Fidel
  • Mora, Leticia
Excel file including: Degree of hydrolysis, antioxidant activity evaluated by DPPH, FRAP and ABTS assays, inhibition of DPP-IV of 3 enzymatic hydrolysates of Spanish dry-cured ham bone, peptide separation by reverse phase chromatography (RP-HPLC) and hydrophilic interaction liquid chromatography (HILIC); peptide identification by mass spectrometry in tandem and free amino acid content of each hydrolysate, The utilization of animal bones as a protein source could be used as a sustainable pathway for the production of bioactive compounds. In this study, bones were pretreated with pepsin enzyme (PEP) and then sequentially hydrolyzed with Alcalase (PA) and Alcalase, as well as Protana prime (PAPP). The degree of hydrolysis, antioxidant activity, and DPP-IV inhibitory activity were measured. All three hydrolysates showed antioxidant and DPP-IV inhibitory activity; however, the highest result in both bioactivities was obtained with the PAPP hydrolysate. The obtained free amino acid content was 54.62, 88.12, and 668.46 mg/100 mL of hydrolyzed in PEP, PA, and PAPP, respectively. Pepsin pretreatment did not significantly affect the degree of hydrolysis; however, it is suggested that it promoted the cleavage of certain bonds for subsequent protease action. Accordingly, a total of 550 peptides were identified in PEP hydrolysate, 1087 in PA hydrolysate, and 1124 in PAPP hydrolysate using an LC-MS/MS approach. Pepsin pretreatment could be an effective method in the utilization of bone sources for the production of antioxidant and hypoglycemic peptides., 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. Grant 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

DOI: http://hdl.handle.net/10261/371528, https://doi.org/10.20350/digitalCSIC/16653
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371528
HANDLE: http://hdl.handle.net/10261/371528, https://doi.org/10.20350/digitalCSIC/16653
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371528
PMID: http://hdl.handle.net/10261/371528, https://doi.org/10.20350/digitalCSIC/16653
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371528
Ver en: http://hdl.handle.net/10261/371528, https://doi.org/10.20350/digitalCSIC/16653
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371528

DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371659
Set de datos (Dataset). 2024

DATA OF MANUSCRIPT PORK ORGANS AS A POTENTIAL SOURCE OF FLAVOUR-RELATED SUBSTANCES

  • López-Martínez, Manuel Ignacio
  • Toldrá Vilardell, Fidel
  • Mora, Leticia
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

DOI: http://hdl.handle.net/10261/371659, https://doi.org/10.20350/digitalCSIC/16657
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371659
HANDLE: http://hdl.handle.net/10261/371659, https://doi.org/10.20350/digitalCSIC/16657
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371659
PMID: http://hdl.handle.net/10261/371659, https://doi.org/10.20350/digitalCSIC/16657
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371659
Ver en: http://hdl.handle.net/10261/371659, https://doi.org/10.20350/digitalCSIC/16657
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371659

DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371666
Set de datos (Dataset). 2024

DATA OF MANUSCRIPT DPP-IV INHIBITORY PEPTIDES GPF, IGL, AND GGGW OBTAINED FROM CHICKEN BLOOD HYDROLYSATES

  • Carrera Alvarado, Gisela
  • Toldrá Vilardell, Fidel
  • Mora, Leticia
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

DOI: http://hdl.handle.net/10261/371666, https://doi.org/10.20350/digitalCSIC/16658
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371666
HANDLE: http://hdl.handle.net/10261/371666, https://doi.org/10.20350/digitalCSIC/16658
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371666
PMID: http://hdl.handle.net/10261/371666, https://doi.org/10.20350/digitalCSIC/16658
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371666
Ver en: http://hdl.handle.net/10261/371666, https://doi.org/10.20350/digitalCSIC/16658
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371666

DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371674
Set de datos (Dataset). 2024

DATA OF MANUSCRIPT EFFECT OF THERMAL PRETREATMENT AND GASTROINTESTINAL DIGESTION ON THE BIOACTIVITY OF DRY-CURED HAM BONE ENZYMATIC HYDROLYZATES

  • Carrera Alvarado, Gisela
  • Toldrá Vilardell, Fidel
  • Mora, Leticia
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

DOI: http://hdl.handle.net/10261/371674, https://doi.org/10.20350/digitalCSIC/16659
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371674
HANDLE: http://hdl.handle.net/10261/371674, https://doi.org/10.20350/digitalCSIC/16659
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371674
PMID: http://hdl.handle.net/10261/371674, https://doi.org/10.20350/digitalCSIC/16659
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371674
Ver en: http://hdl.handle.net/10261/371674, https://doi.org/10.20350/digitalCSIC/16659
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371674

DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371902
Set de datos (Dataset). 2024

DATA OF MANUSCRIPT BILE ACID-BINDING CAPACITY OF PEPTIDE EXTRACTS OBTAINED FROM CHICKEN BLOOD HYDROLYSATES USING HPLC

  • Carrera Alvarado, Gisela
  • Toldrá Vilardell, Fidel
  • Mora, Leticia
Excel file including: Degree of hydrolysis, bile acid binding capacity of nine different enzymatic hydrolysates of chicken blood, total bile acid binding capacity of three peptide fractions of 2 hydrolysates, and density analysis of the SDS-PAGE profile of the >10 kDa fraction of 2 hydrolysates., Bile acids are involved in the modulation of various metabolic processes facilitating the biliary excretion of endogenous and exogenous cholesterol. The objective of this study was to determine the glycocholic acid binding capacity (BC) of chicken blood hydrolysates using an optimized RP-HPLC methodology. Samples were hydrolysed using a combination of five different enzymes. Alcalase and Protamex hydrolysates presented the highest BC, with mean values of 20.09% and 20.61%, respectively. Subsequently, both hydrolysates were ultrafiltered to obtain fractions >10 kDa, between 10 and 3 kDa, and <3 kDa, and the highest BC values were obtained for peptide fractions >10 kDa. Finally, the protein fragments (MW > 10 kDa) potentially responsible for BC were identified by LC-MS/MS. The results confirmed the relation of BC with the molecular weight of the peptides generated, suggesting that certain protein fragments generated from chicken blood could contribute to a positive impact on health by interfering with cholesterol metabolism., Grant PID2020-119684RB-I00 funded by MCIN/AEI/10.13039/501100011033 is acknowledged. Grant GRISOLIAP/2020/021 de la Consellería de Innovacio, Universitats, Ciencia i Societat Digital de la Generalitat Valenciana (GCA) is also acknowledged., Peer reviewed

DOI: http://hdl.handle.net/10261/371902, https://doi.org/10.20350/digitalCSIC/16667
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371902
HANDLE: http://hdl.handle.net/10261/371902, https://doi.org/10.20350/digitalCSIC/16667
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371902
PMID: http://hdl.handle.net/10261/371902, https://doi.org/10.20350/digitalCSIC/16667
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371902
Ver en: http://hdl.handle.net/10261/371902, https://doi.org/10.20350/digitalCSIC/16667
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371902

DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/429002
Set de datos (Dataset). 2026

EXPERIMENTAL DATA OF MANUSCRIPT MICROWAVE IRRADIATION PRE-TREATMENT AS A SUSTAINABLE METHOD TO OBTAIN BIOACTIVE HYDROLYSATES FROM CHICKEN FEATHERS [DATASET]

  • Torices Hernández, Álvaro
  • Gallego, Marta
  • Mora, Leticia
  • Toldrá Vilardell, Fidel
The database includes the information on the results of compositional analysis of chicken feathers and in vitro analysis of six different enzymatic hydrolysates from chicken feathers: C) Control, A) Alcalase 2%, AA) Alcalase 2% + Alcalase 20%, MWC) Microwave Irradiation pre-treatment Control, MWA) Microwave Irradiation pre-treatment Alcalase 2%, MWAA) Microwave Irradiation pre-treatment Alcalase 2% + Alcalase 20%. Antioxidant potential activity, DPP-IV enzyme, Neprolysin enzyme and ACE-I inhibitory activity of the hydrolysates are included. Raw data of identified unique peptide sequences obtained after LC-MS/MS of hydrolysates C, MWC, A and MWA are included., Chicken feathers constitute a major by-product from the poultry industry, with a potential environmental impact and significant difficulties in their management. This study aimed to develop a sustainable method to hydrolyse chicken feathers and evaluate the effects of microwave (MW) irradiation pre-treatment in the generation of bioactive hydrolysates by simple or sequential hydrolysis with Alcalase. The hydrolysate with MW irradiation pre-treatment and Alcalase (2%, 2 h) (MWA) showed the highest overall antioxidant activity and neprilysin-inhibitory activity (55%), whereas samples without MW irradiation pre-treatment exerted the highest inhibitory activity of dipeptidyl peptidase IV (DPP IV) and angiotensin-converting enzyme (ACE-I), with values close to 50 and 70%, respectively. Mass spectrometry in tandem of bioactive hydrolysates was performed, and an in silico approach was used to characterise the obtained sequences. These results confirmed that MW irradiation pre-treatment improved Alcalase hydrolysis, leading to the generation of bioactive peptides with potential multifunctional properties, including antioxidant, antidiabetic, and antihypertensive activities. Moreover, this study highlights the potential of combining MW irradiation and enzymatic hydrolysis as a sustainable strategy for the revalorisation of chicken feathers., Grant PID2023-153058OB-I00 funded by MICIU/AEI/10.13039/501100011033 and FEDER a way of making Europe, and grant PRE2022-105147 to A. Torices-Hernández funded by MICIU/AEI/10.13039/501100011033 and European Social Fund Plus, and the accreditation as Center of Excellence Severo Ochoa CEX2021-001189-S, also funded by MICIU/AEI/10.13039/501100011033, are fully acknowledged., With funding from the Spanish government through the ‘Severo Ochoa Centre of Excellence’ accreditation (CEX2021-001189-S)., Peer reviewed

DOI: http://hdl.handle.net/10261/429002, https://doi.org/10.20350/digitalCSIC/18297
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/429002
HANDLE: http://hdl.handle.net/10261/429002, https://doi.org/10.20350/digitalCSIC/18297
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/429002
PMID: http://hdl.handle.net/10261/429002, https://doi.org/10.20350/digitalCSIC/18297
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/429002
Ver en: http://hdl.handle.net/10261/429002, https://doi.org/10.20350/digitalCSIC/18297
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/429002

RIUMA. Repositorio Institucional de la Universidad de Málaga
oai:riuma.uma.es:10630/32207
Set de datos (Dataset). 2024

DATASET FOR: STUDENT AGGRESSION AGAINST TEACHERS, STRESS, AND EMOTIONAL INTELLIGENCE AS PREDICTORS OF WITHDRAWAL INTENTIONS AMONG SECONDARY SCHOOL TEACHERS.

DATASET_AGGRESSION_WITHDRAWAL_TEACHERS

  • Mérida-López, Sergio
  • Extremera-Pacheco, Natalio
Background and Objectives: This exploratory study aimed to test the buffering effect of emotional intelligence in the associations between aggression against teachers, perceived stress, and withdrawal intentions. Design and Methods: A sample of 329 secondary school teachers (51.4% female) completed questionnaires assessing aggression against teachers, perceived stress, withdrawal intentions, and emotional intelligence. Results: The results showed that emotional intelligence was negatively related to perceived stress and withdrawal intentions. Across moderated-mediation analysis, there were mixed findings regarding the moderating effects of emotional intelligence in the proposed model. Findings indicated that emotional intelligence moderated only the association between perceived stress and withdrawal intentions. Conclusions: These findings suggest that emotional intelligence is a psychological resource for mitigating the negative effects of perceived stress on negative work attitudes among teaching professionals in the context of harmful student behaviors. Possible avenues for including emotional intelligence in the field of teacher victimization are discussed., -Ayuda predoctoral del Ministerio de Educación, Cultura y Deporte (FPU16/02238) -Universidad de Málaga y Junta de Andalucía (UMA18-FEDERJA-147) -Grupo PAIDI CTS-1048 de la Junta de Andalucía

Proyecto: //
DOI: https://hdl.handle.net/10630/32207
RIUMA. Repositorio Institucional de la Universidad de Málaga
oai:riuma.uma.es:10630/32207
HANDLE: https://hdl.handle.net/10630/32207
RIUMA. Repositorio Institucional de la Universidad de Málaga
oai:riuma.uma.es:10630/32207
PMID: https://hdl.handle.net/10630/32207
RIUMA. Repositorio Institucional de la Universidad de Málaga
oai:riuma.uma.es:10630/32207
Ver en: https://hdl.handle.net/10630/32207
RIUMA. Repositorio Institucional de la Universidad de Málaga
oai:riuma.uma.es:10630/32207

DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/205462
Set de datos (Dataset). 2020

DATA ON BIOACTIVE PEPTIDES DERIVED FROM CHICKEN HYDROLYSATE WITH POTENTIAL ALCOHOL DEHYDROGENASE STABILIZING ACTIVITY AND IN SILICO ANALYSIS OF THEIR POTENTIAL ACTIVITY AND APPLICABILITY

  • Xiao, C.
  • Zhao, M.
  • Zhou, F.
  • Gallego, Marta
  • Toldrá, Fidel
  • Mora, Leticia
Refers to: Chuqiao Xiao, Mouming Zhao, Feibai Zhou, Marta Gallego, Jie Gao, Fidel Toldrá, Leticia Mora. Isolation and identification of alcohol dehydrogenase stabilizing peptides from Alcalase digested chicken breast hydrolysates. Journal of Functional Foods 64:103617 (2020), Bioactive peptides have attracted extensive attention worldwide as natural alternatives to promote human health and wellness. Previous studies have shown that chicken hydrolysates could enhance alcohol dehydrogenase, and subsequently they facilitate alcohol metabolism and ameliorate alcohol-induced liver injury. The data presented in this article support the accompanying research article “Isolation and identification of alcohol dehydrogenase stabilizing peptides from Alcalase digested chicken breast hydrolysates”. Present article details all 82 peptides identified from the most active fractions of chicken hydrolysates, and 154 peptides from in silico digestion of the 82 identified peptides, together with the prediction of their potential bioactivity and applicability using several in silico assays., This work was supported by Grant AGL2017-89381-R and FEDER funds from the Spanish Ministry of Economy, Industry and Competitiveness, the National Natural Science Foundation of China (No. 31701539 and No.31871746) and the Natural Science Foundation of Guangdong Province (No. 2017A030313127). We also thank Ramón y Cajal postdoctoral contract by L.M. and the China Scholarship Council (CSC) research program for providing funding for C. X., Peer reviewed

DOI: http://hdl.handle.net/10261/205462
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/205462
HANDLE: http://hdl.handle.net/10261/205462
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/205462
PMID: http://hdl.handle.net/10261/205462
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/205462
Ver en: http://hdl.handle.net/10261/205462
DIGITAL.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/205462

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