Identification and Quantitation of Bioactive and Taste-Related Dipeptides in Low-Salt Dry-Cured Ham

The reduction of salt in meat products influences the natural mechanisms of proteolysis occurring in their processing, and could affect the final characteristics of the product in terms of texture and flavor due to its effect on the activity of enzymes. In the present study, the quantitation of dipeptides PA, GA, VG, EE, ES, DA, and DG in low-salt Spanish dry-cured ham was carried out using a triple quadrupole mass spectrometry instrument. The developed methodology demonstrated the advantages of hydrophilic interaction liquid chromatography in the removal of salt as a clean-up/separation step before ionization. This resulted in a value of 44.88 μg/g dry-cured ham for GA dipeptide, and values ranging from 2 to 8 μg/g dry-cured ham for VG, EE, ES, DA, and DG dipeptides. PA showed the lowest concentration with a value of 0.18 μg/g dry-cured ham. These outcomes prove the remarkable activity of muscular dipeptidyl peptidases during dry-curing as well as confirming the presence of these dipeptides which are related to certain taste attributes (e.g., 'bitter' or 'umami'). Such dipeptides have also been confirmed as anti-inflammatory and potential cardiovascular protectors using in vitro assays, with the advantage of dipeptides small size increases their chance to resist both gastrointestinal digestion and intestinal/bloodstream transport without being degraded or modified.

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Bibliographic Details
Main Authors: Heres, Alejandro, Gallego, Marta, Mora, Leticia, Toldrá Vilardell, Fidel
Other Authors: Ministerio de Ciencia e Innovación (España)
Format: artículo biblioteca
Language:English
Published: Multidisciplinary Digital Publishing Institute 2022-02-24
Subjects:Bioactivity, Curing, Dry-cured ham, Mass spectrometry, Meat products, Peptides, Peptidomics, Triple quadrupole,
Online Access:http://hdl.handle.net/10261/263714
http://dx.doi.org/10.13039/501100000780
http://dx.doi.org/10.13039/501100004837
https://api.elsevier.com/content/abstract/scopus_id/85125063250
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