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不同的肌原纤维亚蛋白组谱与陈年猪里脊肉的仪器质地有关。

Distinct myofibrillar sub-proteomic profiles are associated with the instrumental texture of aged pork loin.

机构信息

Department of Animal Science, Iowa State University, Ames, IA 50011, USA.

Department of Animal Science, University of Connecticut, Storrs, CT 06269-4040, USA.

出版信息

J Anim Sci. 2023 Jan 3;101. doi: 10.1093/jas/skad327.

Abstract

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.

摘要

新鲜猪肉的嫩度是消费者对食用体验满意的关键。肌原纤维内和肌原纤维间蛋白质的死后降解与猪肉嫩度的发展密切相关。清楚地了解与猪肉嫩度发展相关的分子特征将提供额外的目标,并为改善和使猪肉嫩度发展更加一致开辟新的解决方案。因此,本研究旨在利用液相色谱-串联质谱和串联质量标签(TMT)多重化技术,评估不同仪器星探针值猪排之间肌原纤维亚蛋白组的差异。在死后 24 小时,从商业收获设施中收集猪里脊肉(N=120)。在死后 24 小时和大约 2 周的尸僵老化后评估肉质和感官特性。根据仪器星探针值将猪排分为 4 组(组 A,x¯=4.23 kg,3.43-4.55 kg;组 B,x¯=4.79 kg,4.66-5.00 kg;组 C,x¯=5.43 kg,5.20-5.64 kg;组 D,x¯=6.21 kg,5.70-7.41 kg;每组 25 个样本)。将老化约 2 周的样本中的肌原纤维蛋白进行分级、洗涤,然后在 8.3 M 尿素、2 M 硫脲和 1%二硫苏糖醇中溶解。用胰蛋白酶消化蛋白质,用 11 重同位素标记的 TMT 试剂标记,并使用 Q-Exactive 质谱仪进行鉴定和定量。在组 A 和组 D 之间,有 54 种蛋白质组存在差异丰度(调整后 P<0.05)。与组 D 相比,组 A 的厚肌丝和薄肌丝相关蛋白丰度更高,Z 线相关蛋白和代谢酶丰度更低。这些数据表明,不同嫩度值的猪排与不同的肌原纤维亚蛋白组有关。未来的研究应该评估死后立即和更早的变化,以进一步阐明死后老化过程中肌原纤维亚蛋白组的差异。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/92bf/10629443/ec2884977e83/skad327_fig1.jpg

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