新鲜猪肉的嫩度有助于消费者对饮食体验的满意度。肌原纤维内部和之间蛋白质的死后蛋白水解与猪肉嫩度的发展密切相关。对与猪肉嫩度发展相关的分子特征的清晰了解将提供额外的目标,并为改善和使猪肉嫩度发展更加一致的新解决方案打开大门。因此,目的是利用具有串联质量标签(TMT)复用的液相色谱和质谱来评估不同仪器星形探针值的猪排之间的肌原纤维亚蛋白质组差异.在死后24小时从商业收获设施收集猪腰(N=120)。在死后24小时和死后老化约2周后评估质量和感官属性。根据仪器星探值将猪排分为4组(A组,x'=4.23kg,3.43-4.55千克;B组,x'=4.79kg,4.66-5.00kg;C组,x'=5.43kg,5.20-5.64kg;D组,x'=6.21kg,5.70-7.41千克;每组n=25)。来自大约2周龄的样品的肌原纤维蛋白被分级分离,washed,并溶解在8.3M尿素中,2M硫脲,和1%二硫苏糖醇。蛋白质用胰蛋白酶消化,用11-plex等压TMT试剂标记,并使用Q-Exactive质谱仪进行鉴定和定量。在A组和D组之间,54个蛋白质组差异丰富(调整后的P<0.05)。与D组印章相比,A组与粗细细丝相关的蛋白质丰度更高,而Z线相关蛋白质和代谢酶的丰度更低。这些数据强调了不同的肌原纤维亚蛋白质组与不同嫩度值的猪排相关。未来的研究应该立即和更早地评估死后的变化,以进一步阐明死后衰老期间肌原纤维亚蛋白质组的差异。
Fresh pork tenderness contributes to consumer satisfaction with the eating experience. Postmortem proteolysis of proteins within and between myofibrils has been closely linked with pork tenderness development. A clear understanding of the molecular features associated with pork tenderness development will provide additional targets and open the door to new solutions to improve and make pork tenderness development more consistent. Therefore, the objective was to utilize liquid chromatography and mass spectrometry with tandem mass tag (TMT) multiplexing to evaluate myofibrillar sub-proteome differences between pork chops of different instrumental star probe values. Pork loins (N = 120) were collected from a commercial harvest facility at 24 h postmortem. Quality and sensory attributes were evaluated at 24 h postmortem and after ~2 weeks of postmortem aging. Pork chops were grouped into 4 groups based on instrumental star probe value (group A,x¯ = 4.23 kg, 3.43 to 4.55 kg; group B,x¯ = 4.79 kg, 4.66 to 5.00 kg; group C,x¯ = 5.43 kg, 5.20 to 5.64 kg; group D,x¯ = 6.21 kg, 5.70 to 7.41 kg; n = 25 per group).
Myofibrillar proteins from the samples aged ~2 wk were fractionated, washed, and solubilized in 8.3 M urea, 2 M thiourea, and 1% dithiothreitol. Proteins were digested with trypsin, labeled with 11-plex isobaric TMT reagents, and identified and quantified using a Q-Exactive Mass Spectrometer. Between groups A and D, 54 protein groups were differentially abundant (adjusted P < 0.05). Group A had a greater abundance of proteins related to the thick and thin filament and a lesser abundance of Z-line-associated proteins and metabolic enzymes than group D chops. These data highlight that distinct
myofibrillar sub-proteomes are associated with pork chops of different tenderness values. Future research should evaluate changes immediately and earlier postmortem to further elucidate
myofibrillar sub-proteome differences over the postmortem aging period.
A primary goal of meat production is to efficiently produce safe, high-quality products. Competing interests within the goal complicate this seemingly simple aspiration. Consequently, it is necessary to emphasize efforts to enhance our comprehension of biological and molecular factors that influence quality, safety, and efficient meat production. This experiment aimed to define the proteomic profiles of the
myofibrillar fraction of fresh pork with differing quality traits. Myofibrils from aged pork chops with a range of tenderness levels were used to achieve this objective. Fifty-four proteins were differentially abundant between the divergent tenderness groups. This was due to the expression profile of proteins in muscle and/or changes in proteins in the
myofibrillar fraction during postmortem aging. These results inform and direct the development of antemortem and postmortem applications to ensure success in producing high-quality pork.