Related Experiment Video
Updated: Aug 11, 2026

Introducing an Angle Adjustable Cutting Box for Analyzing Slice Shear Force in Meat
Published on: April 26, 2013
Distinct myofibrillar sub-proteomic profiles are associated with the instrumental texture of aged pork loin
Logan G Johnson1, Chaoyu Zhai2, Edward M Steadham1
1Department of Animal Science, Iowa State University, Ames, IA 50011, USA.
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.
More Related Videos
09:29Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
Published on: May 18, 2017
07:46Author Spotlight: Improving Beef Cattle Nutrition and Production with a Focus on Feed Efficiency and Meat Quality Traits Through Advanced Biochemical and Molecular Assays
Published on: July 12, 2024
Related Concept Videos
Protein Organization
Bone Structure
Collagens are the Major Structural Proteins of ECM
Connective tissue proper includes loose...
The Bone Matrix
Spongy Bone
Spongy bone is more porous, and less dense compared to compact bone. It is composed of concentric lamellae that are arranged irregularly to form the trabecular network. In some bones, the spaces between trabeculae contain red marrow, where...
Fibrous Proteins