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Ripoll G - Autor o Coautor
Publicaciones > Artículo

A proteomic approach for in-depth characterization and understanding the impact of immunocastration on dry-cured ham of male and female pigs

Publicado en:Food Research International. 154 111020- - 2022-04-01 154(), doi: 10.1016/j.foodres.2022.111020

Ripoll G;


Centro de Investigaci?n y Tecnolog?a Agroalimentaria de Arag?n - Autor o Coautor
Centro de Investigación y Tecnología Agroalimentaria de Aragón - Entidad de origen
CYTED Ciencia y Tecnología para el Desarrollo - Financiador
Facultad de Veterinaria, Universidad de Zaragoza - Autor o Coautor
Fundación Centro Tecnolóxico da Carne - Autor o Coautor
Fundación Centro Tecnolóxico da Carne , Universidade de Vigo - Autor o Coautor
Universidad de Santiago de Compostela - Autor o Coautor
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Resúmen: Dry-cured ham is a high-quality product elaborated through a long and complex process. To ensure the success of the process, it is necessary to select the most suitable pork leg and one of the major factors is pig castration. Due to animal welfare, pig castration is becoming a paramount issue in recent years. The proteomic differences of dry-cured ham from immunecastrated pigs against entire females, as well as, between immunecastrated pigs and surgically castrated males were analysed. The identification and quantification of proteins were carried out by sequential window acquisition of all theoretical mass spectra (SWATH-MS). A total of 249 proteins were identified across the samples of dry-cured ham, resulting in 17 and 37 differentially abundant proteins in the case of males and females, respectively. In the case of males, a high abundance of structural proteins in dry-cured ham from surgically castrated animals as well as a high abundance of trypsinogen and proteosome subunit C9-like protein with protease activity in samples from immunocastrated males suggests that immunocastration impact on myofibrils of dry-cured ham. Regarding females, the immunocastration provoked an increase of abundance in several structural proteins of the myosin heavy chain (MYH7, MYH7B and MYH4) and a decrease in others (ACTN2, TNNT3, MYL3 and TCAP) concerning entire. Overall, MYH4 and ACT were found to a greater degree in immunocastrated males and females indicating a potential for biomarkers.

Palabras clave: animal welfare; myofibrillar proteins; myosin heavy chain; processed products; protein biomarkers; Animal welfare; Myofibrillar proteins; Myosin heavy chain; Processed products; Protein biomarkers; Protein modifications

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