Capillary liquid-chromatography-ion trap-mass spectrometry methodology for the simultaneous quantification of four angiotensin-converting enzyme-inhibitory peptides in Prunus seed hydrolysates
IdentifiersPermanent link (URI): http://hdl.handle.net/10017/44847
AffiliationUniversidad de Alcalá. Departamento de Química Analítica, Química Física e Ingeniería Química
Journal of Chromatography A., 2018, v. 1540, p. 47-54
ACE inhibitory peptides
Ion trap mass spectrometry
Ministerio de Economía y Competitividad de España (Ref. AGL2016-79010-R) y la Comunidad Autónoma de Madrid y financiación europea del programa FEDER (S2013 / ABI-3028, AVANSECAL-CM).
Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
Prunus genus fruit seeds are sources of highly angiotensin-l-converting enzyme (ACE)-inhibitory peptides. The presence of peptides IYSPH, IYTPH, IFSPR, and VAIP seems to be related to this activity but no previous work has demonstrated the direct relationship between the concentration of these peptides and the antihypertensive activity of hydrolysates. This work describes the development of a method for the quantification of these peptides in Prunus seeds hydrolysates based on capillary liquid chromatography-IT-MS/MS. The analytical characteristics of the method were evaluated through the study of the linearity, LOD, LOQ presence of matrix interferences, precision, and recovery. The developed methodology was applied to the determination of the four peptides in seed hydrolysates from different Prunus genus fruits: peaches (7 varieties), plums (2 varieties), nectarines (3 varieties), apricots (2 varieties), cherry, and paraguayo. Peaches and plums seed hydrolysates yielded the highest concentrations of these peptides while paraguayo one showed the lowest concentrations. A high correlation between peptides concentrations was demonstrated suggesting that the four peptides could be released from the same seed proteins.
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