RT info:eu-repo/semantics/article T1 Capillary liquid-chromatography-ion trap-mass spectrometry methodology for the simultaneous quantification of four angiotensin-converting enzyme-inhibitory peptides in Prunus seed hydrolysates A1 González García, Estefanía A1 García López, María Concepción A1 Marina Alegre, María Luisa K1 ACE inhibitory peptides K1 Quantification K1 Capillary-HPLC K1 Ion trap mass spectrometry K1 Prunus seeds K1 Química K1 Chemistry AB 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. SN 0021-967 YR 2018 FD 2018-03-09 LK http://hdl.handle.net/10017/44847 UL http://hdl.handle.net/10017/44847 LA eng DS MINDS@UW RD 29-mar-2024