ABSTRACT
During cutting and processing of meat, the loss of water is critical in determining both product quality and value. From the point of slaughter until packaging, water is lost due to the hanging, movement, handling, and cutting of the carcass, with every 1% of lost water having the potential to cost a large meat processing plant somewhere in the region of 50,000 per day. Currently the options for monitoring the loss of water from meat, or determining its drip loss, are limited to destructive tests which take 24-72 h to complete. This paper presents results from work which has led to the development of a novel microwave cavity sensor capable of providing an indication of drip loss within 6 min, while demonstrating good correlation with the well-known EZ-Driploss method (R² = 0.896).
Subject(s)
Biosensing Techniques/instrumentation , Food Analysis , Food Quality , Meat , Animals , Swine , Water/analysisABSTRACT
Heparin-binding proteins in human plasma were studied using affinity chromatography columns with porcine (2mL, 10.7mg capacity) and piscine heparin (5mL, 2.7mg capacity). Two-dimensional electrophoresis (Bio-Rad Protean II gel system with 16cm×16cm gels using isoelectric focusing (IEF) and nonequilibrium pH-gradient gel electrophoresis (NEPHGE)), Bruker Ultraflex MALDI-TOF mass spectrometry and immunoblotting (NovaBlot semidry discontinuous blotting) were used for unfractionated plasma. This revealed electropherograms with differences between porcine and piscine heparin-binding and totally 17 different fibrinogen variants from all 3 chains. Immunodepletion was used to remove fibrinogen (42.1mg anti-human fibrinogen in 8.4mL resin) and serum albumin (0.42mg binding capacity in 14mL resin) and porcine and piscine heparin-binding proteins were identified using liquid chromatography-mass spectrometry (Ultimate 3000 NanoLC with Acclaim PepMap 100 column (50cm×75µm)-LTQ Orbitrap Mass XL). In total, the binding of 76 putative or acknowledged biomarkers are shown. Of the identified proteins, 14 are not previously shown to be heparin-binding, such as the low concentration proteins lipocalin-1 and tropomyosin and a hitherto not detected protein in plasma, zinc finger protein 483. The putative heparin-binding sequences were analyzed. The results suggest that the combination of group specific affinity and adapted immunodepletion chromatography could be useful in the study of the plasma proteome.
Subject(s)
Blood Proteins/analysis , Blood Proteins/metabolism , Chromatography, Affinity/methods , Heparin/metabolism , Immobilized Proteins/metabolism , Animals , Blood Proteins/chemistry , Electrophoresis, Gel, Two-Dimensional/methods , Fish Proteins/chemistry , Fish Proteins/metabolism , Heparin/chemistry , Humans , Immobilized Proteins/chemistry , Immunosorbent Techniques , Mass Spectrometry , Salmo salar , SwineABSTRACT
Changes induced by low-voltage electrical stimulation (ES; 0-95 V for 8 s; 95 V for 32 s) in the insoluble protein fraction of bovine longissimus dorsi (LD) muscle at 1 and 24h post-ES were investigated by proteomics. Protein abundance patterns from ten Norwegian Red (NRF) young bulls were compared, and significant changes due to ES were found by rotation test and partial least square (PLS) regression analyses. Five protein spots showed lower abundance in ES samples at both sampling times, and in addition, 10 proteins at 1 h post-ES and 13 proteins at 24 h post-ES changed significantly in abundance due to ES. Reduced abundance of full-length structural proteins in ES samples indicates an accelerated proteolysis due to ES. Moreover, increased abundance of small heat shock proteins indicates earlier initiation of stress responses due to ES. These findings provide a better understanding of the biochemical processes taking place as a result of ES during post mortem storage of meat.
Subject(s)
Actins/analysis , Meat , Muscle, Skeletal/chemistry , Proteome/analysis , Actins/chemistry , Actins/metabolism , Animals , Cattle , Creatine Kinase/metabolism , Desmin/analysis , Desmin/chemistry , Desmin/metabolism , Electric Stimulation/methods , Electrophoresis, Gel, Two-Dimensional , Food Preservation/methods , Heat-Shock Proteins/analysis , Male , Mass Spectrometry , Myofibrils/chemistry , Proteome/metabolism , Proteomics , Troponin T/analysis , Troponin T/chemistry , Troponin T/metabolism , alpha-Crystallins/analysis , alpha-Crystallins/chemistry , alpha-Crystallins/metabolismABSTRACT
Changes in the insoluble protein fraction of bovine longissimus thoracis muscle from eight Norwegian Red (NRF) dual-purpose young bulls during the first 48 h postmortem were investigated by two-dimensional gel electrophoresis (2DE) and matrix-assisted laser desorption ionization-time of flight tandem mass spectrometry (MALDI-TOF MS/MS). Significant changes were observed in a total of 35 proteins, and of those, 26 were identified and divided into three different groups: metabolic enzymes, cellular defense/stress proteins, and structural proteins, according to their predicted function. The majority of the metabolic enzymes identified are involved in the energy metabolism of the cell, while the cellular defense/stress proteins can be related to regulation and stabilization of the myofibrillar proteins. Both easily soluble proteins as well as structural proteins were identified in the insoluble protein fraction. We have studied the changes in solubility during postmortem storage by comparing the postmortem changes in protein composition between the soluble and insoluble protein fractions. We have identified two metabolic enzymes (2,3-bisphosphoglycerat mutase and NADH dehydrogenase) and one protein involved in the stress responses/apoptosis of the cell (Hsp70) that have not been identified previously in the insoluble protein fraction. The occurrence of these easily soluble proteins in the insoluble protein fraction could be due to precipitation or aggregation, thereby going from a soluble to an insoluble state.
