Dataset.
Data of manuscript Bile acid-binding capacity of peptide extracts obtained from chicken blood hydrolysates using HPLC
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371902
Digital.CSIC. Repositorio Institucional del CSIC
- 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
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371902
HANDLE: http://hdl.handle.net/10261/371902
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371902
Ver en: http://hdl.handle.net/10261/371902
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371902
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Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/371902
Dataset. 2024
DATA OF MANUSCRIPT BILE ACID-BINDING CAPACITY OF PEPTIDE EXTRACTS OBTAINED FROM CHICKEN BLOOD HYDROLYSATES USING HPLC
Digital.CSIC. Repositorio Institucional del CSIC
- 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
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