Proteomic Profiles of the Longissimus Muscles of Entire Male and Castrated Pigs as Related to Meat Quality

• Published in: Animals (Basel) Vol. 9; no. 3; p. 74
• Main Authors: Škrlep, Martin, Tomažin, Urška, Lukač, Nina Batorek, Poklukar, Klavdija, Čandek-Potokar, Marjeta
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 27.02.2019; MDPI
• Subjects: Actin; Aggressiveness; Blood plasma; Carbonyl compounds; Carbonyl groups; Carbonyls; castrates; Collagen; Cooking; entire males; Etiology; Heat shock proteins; Hogs; Malate dehydrogenase; Meat; Meat quality; Muscles; Myosin; Oxidation; pigs; Plasma proteins; Proteins; Proteolysis; proteomic profile; Sweden; Slovenia; United States > US; Germany; meat quality; castrates; pigs; proteomic profile; entire males
• ISSN: 2076-2615; 2076-2615
• DOI: 10.3390/ani9030074

There are indications of reduced meat quality in entire male pigs (EMs) in comparison to surgically castrated pigs (SCs); however, the differences are not strongly confirmed, and the etiology is not clarified. In the present study, samples of the longissimus dorsi, pars lumborum muscle (LL) from EMs ( = 12) and SCs ( = 12) of the same age and weight were evaluated at the physico-chemical and proteomic level. EMs exhibited lower intramuscular fat content, higher collagen content with higher solubility, a higher level of protein carbonyl groups (indicating higher protein oxidation), lower water holding capacity, and tougher meat than SCs. Proteomic analysis revealed differences in heat shock proteins expression, while a greater abundance of several other identified proteins (malate dehydrogenase, Na/K-transporting adenosintriphosphatase (ATP-ase) subunit alpha-1, and blood plasma proteins) indicates that EMs have a more oxidative metabolic profile than that of SCs. More abundant protein fragments (mainly actin and myosin heavy chain) suggest a higher degree of proteolysis in EMs, which was not followed by lower meat toughness.