Synergistic effects of psyllium husk powder and different levels of methylcellulose on the storage stability of sodium caseinate emulsion.

The study investigated the effects of compound fibers composed of psyllium husk powder (PHP, 0.3%) and methylcellulose (MC, 0, 0.3, 0.6, 0.9, and 1.2%) on the storage stability, rheology, and microstructure of sodium caseinate emulsions. Results showed that the emulsion stability was enhanced with the increased concentrations of MC, especially at the concentration of 1.2%. The oil droplet size in the emulsions was decreased as the concentrations of compound fibers increased, which was further confirmed by the optical microscope analysis. The rheological measurements and cryo-scanning electron microscopy results indicated that compound fibers improved the viscosity of the emulsions, and formed a strong three-dimensional network structure. The results of confocal laser scanning microscope and surface protein concentration measurements showed that compound fibers were evenly distributed into the oil droplet surface. The above results demonstrate that compound fibers are an effective thickener and emulsifier in enhancing the stability properties of oil-in-water (O/W) emulsions stabilized by sodium caseinate.

In Vitro Susceptibility of Oxidized Myosin by µ-Calpain or Caspase-3 and the Determination of the Oxidation Sites of Myosin Heavy Chains.

The effect of susceptibility to in vitro oxidation on the degradation of myosin isolated from beef muscles via µ-calpain or caspase-3 was examined, and the measurement of the oxidation sites of myosin heavy chains was performed. Myosin was incubated with hydroxyl free radical-generating systems, which were composed of 0.01 M FeCl3, 0.1 M ascorbic acid, and 0, 25, 50, and 100 µM H2O2 at 37 °C for 20 min. The oxidized myosin then reacted with µ-calpain or caspase-3 at 37 °C for 30 min, respectively. The results showed that protein oxidation systems in vitro resulted in different levels of myosin oxidation, leading to significant changes in the secondary structure of myosin (P < 0.05). The sodium dodecyl dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting results showed that in vitro oxidation promoted myosin degradation via µ-calpain or caspase-3. Proteomics research suggested that the number of myosin oxidation sites increased constantly with the increase of oxidation levels. Oxidation sites of myosin were mainly cysteine, methionine, arginine, histidine, tyrosine, lysine, and asparagine. These results indicated that oxidation using H2O2 in the range of 0-100 µM could increase the degradation of myosin via µ-calpain and caspase-3 due to increased exposure of the oxidation sites of myosin.

Influence of modified atmosphere packaging on protein oxidation, calpain activation and desmin degradation of beef muscles.

BACKGROUND: Protein oxidation is widespread in biochemical systems. The objective of the study was to investigate the differences in protein oxidation, µ-calpain activity, desmin proteolysis and protein solubility of beef psoas major (PM) and semi-membranosus (SM) muscles under three packaging systems during postmortem ageing. At 24 h postmortem, beef muscles were packaged respectively in air-permeable film overwrap (AP), vacuum pack (VP) or modified atmosphere (MAP, 80% O2 + 20% CO2 ), and then displayed for 10 days at 4 °C. RESULTS: Carbonyl group values and thiol group content were significantly influenced by packaging type and storage time. The SM muscles from AP and MAP showed greater µ-calpain activity compared to VP. Desmin of PM and SM from AP and MAP samples showed decreased proteolysis compared with VP. CONCLUSION: The results suggested that the inhibition of µ-calpain activity of beef samples from AP and MAP could be closely associated with protein oxidation which further lowered the level of desmin degradation compared to VP. © 2017 Society of Chemical Industry.

Differences in calpain system, desmin degradation and water holding capacity between commercial Meishan and Duroc × Landrace × Yorkshire crossbred pork.

The objective of this study was to examine the differences in calpain system, desmin degradation, pH values and water holding capacity (WHC) between muscles of commercial Meishan and Duroc × Landrace × Yorkshire crossbred pigs. Meishan pork presented better WHC evidenced by lower purge loss at days 1 and 3 and less centrifugation loss at day 1 post mortem (P < 0.05). pH values at 45 min post mortem in Meishan pork were significantly higher compared to crossbred pork (P < 0.05). Calpain-1 messenger RNA (mRNA) expression was lower in Meishan pork compared to that from crossbred pork (P < 0.05). Additionally, calpain-1 activity, the ratio of calpain-1 to calpastatin activity and desmin degradation were lower in Meishan pork compared to those from crossbred pork samples (P < 0.05). The results indicate that the calpain system including mRNA expression and activity were different between commercial Meishan and crossbred pork resulting in difference in the degree of desmin degradation during post mortem aging. pH values at 45 min and 24 h post mortem rather than calpain activity and desmin degradation could explain the higher water holding capacity in commercial Meishan pork.

Activity and expression of nitric oxide synthase in pork skeletal muscles.

The objective of this study was to investigate the biochemical changes of nitric oxide synthase (NOS) in pork skeletal muscles during postmortem storage. Longissimus thoracis (LT), psoas major (PM) and semimembranosus (SM) muscles of pork were removed immediately after slaughter and stored under vacuum condition at 4°C for 0, 1 and 3d. Results showed that all three muscles exhibited NOS activity until 1d while SM muscle retained NOS activity after 3d of storage. The content of nNOS in SM muscle was stable across 3d of storage while decreased intensity of nNOS was detected at 1 and 3d of aging in PM and LT muscles due to the degradation of calpain. Immunostaining showed that nNOS was located at not only sarcolemma but also cytoplasm at 0 and 1d of storage. Our data suggest that postmortem muscles possess NOS activity and nNOS expression depends on muscle type.

Effect of nitric oxide on µ-calpain activation, protein proteolysis, and protein oxidation of pork during post-mortem aging.

The aim of the current research was to examine the influence of nitric oxide (NO) on calpain activation, protein proteolysis, and oxidation in post-mortem pork. Five longissimus muscles were removed from carcass after slaughter, and samples were incubated with water, nitric oxide synthase (NOS) inhibitor, or NO donor for 24 h at 4 °C. The samples were taken out and then stored under 4 °C for 1, 4, and 7 d. Results showed that autolysis of µ-calpain increased by incubation with NOS inhibitor after storage for 1 d (P<0.05). Degradation of titin and nebulin increased by treatment of NOS inhibitor among three treatments (P<0.05). Higher levels of protein oxidation were observed after samples incubated with NO donor than treatment of NOS inhibitor (P<0.05). These data indicated that NO could participate in regulating calpain activation and its proteolysis activity during post-mortem aging.

[Research progresses of the synthesis and application of oligopeptide containing Arg-Gly-Asp sequence].

Arg-Gly-Asp (RGD) is one of the oligopeptides with biological activity found in recent years. It is the minimum ammonia serial on the ligand, which can be recognized by most of the integrins. It has important influence on the recognition of endothelial cell, anti-thrombus and anti-tumour function, and the therapy of burn and skin helcosis. In this review, the synthesis and application of oligopeptide [correction of oligepoptide] containing RGD sequence were discussed.