Fish processing has serious economic and environmental costs in the food supply chain. It is necessary to find new ways to convert fish residue to added-value products, especially for main aquaculture species. In this study, a pulsed electric field (PEF) process for antioxidant extract production from three residues (gills, bones, and heads) of two commercial species (sea bream and sea bass) was tested. Three methods of extraction using two solvents (water and methanol) and a water extraction assisted by PEF were assessed. Chemical and mineral compositions, as well as amino acid profile of the by-products, were determined. In addition, four in vitro antioxidant methods, 2,2-diphenyl-1-picrylhydrazyl radical scavenging activity (DPPH), 2,2-azinobis-(3-ethyl-benzothiazoline-6-sulphonate radical (ABTS), ferric reducing antioxidant power assay (FRAP), and oxygen radical absorbance capacity assay (ORAC), were used to evaluate the extracts. Antioxidant activity was confirmed by DPPH and ABTS and FRAP tests, obtaining the highest values for residues from the sea bream species. ORAC values were higher in methanol than in water solvent. In general, gills were the residues with the greatest antioxidant activity for the four antioxidant assays employed. For DPPH assay, the extracts of water assisted by PEF from heads, bones, and gills yielded significant increases of 35.8%, 68.6%, and 33.8% for sea bream and 60.7%, 71.8%, and 22.1% for sea bass, respectively, with respect to water extracts. Our results suggest that PEF would be an environmentally friendly and economic choice for antioxidant-extract production from low-value by-products from fish processing.

Different health institutions from western countries ha–ve recommended a diet higher in polyunsaturated fats, especially of the n-3 family. However, this is not a trivial task, especially for meat-processing sectors. The objective of this work was to assess the influence of replacing pork backfat with linseed oleogel on the main quality parameters of frankfurters. The frankfurters were formulated by the pork backfat replacement of 0% (control), 25% (SF-25), and 50% (SF-50), using a linseed oleogel gelled with beeswax. The determination of quality parameters (pH, colour, chemical composition, and texture parameters), the fatty acid profile, and the sensory evaluation was carried out for each batch. The fatty acid profile was substantially improved, and the saturated fatty acid (SFA) content was reduced from 35.15g/100g in control sausages to 33.95 and 32.34g/100 g in SF-25 and SF-50, respectively, and more balanced ratios n-6/n-3 were achieved. In addition, the sausages with linseed oleogel also decreased the cholesterol content from 25.08 mg/100 g in control sausages to 20.12 and 17.23 mg/100 g in SF-25 and SF-50, respectively. It may therefore be concluded that these innovative meat products are a healthier alternative. However, sensory parameters should be improved in order to increase consumer acceptability, and further research is needed.

Pre-slaughter stress has adverse effects on meat quality that can lead to the occurrence of Dark Firm Dry (DFD) meat in cattle. This study explores the previously uncharacterized proteome changes linked to pre-slaughter stress in the longissimus thoracis (LT) bovine muscle. Differential proteome profiles of DFD and normal (non-DFD) LT meat samples from male calves of the Rubia Gallega breed were assessed by 2-DE coupled to MS analysis (LC-MS/MS and MALDI TOF/TOF MS). A total of seven structural-contractile proteins (three different myosin light chain isoforms, two fast skeletal myosin light chain 2 isoforms, troponin C type 2 and cofilin-2) and three metabolism enzymes (triosephosphate isomerase, ATP synthase and beta-galactoside alpha-2,6-sialyltransferase) were found to have statistically significant differential abundance in sample groups. In addition, 2-DE in combination with the phosphoprotein-specific fluorescent dye Pro-Q DPS revealed that highly phosphorylated fast skeletal myosin regulatory light chain 2 isoforms underwent the most intense relative change in muscle conversion to DFD meat. Therefore, they appear to be the most sensitive biomarkers of stress just prior to slaughter in Rubia Gallega. Overall, these findings will facilitate a more integrative understanding of the biochemical processes associated with stress in cattle muscle and their effects in meat quality. Pre-slaughter stress is a crucial factor in meat production. Animals destined for slaughter are stressed by a variety of endogenous and exogenous factors that negatively affect the complex post-mortem biochemical events underlying the conversion of muscle into meat. The study of the muscle proteome has a great relevance for understanding the molecular mechanisms associated with stress. However, there is no information available on the molecular changes linked to pre-slaughter stress in cattle on the proteome scale. Our study led to the identification of a number of candidate proteins associated with the response to pre-slaughter stress in the LT bovine muscle of the Rubia Gallega breed. The functions of those significantly changed proteins have a clear biological relationship with stress response. These findings contribute to a deeper insight into the molecular pathways that respond to stress in cattle.

Food allergies are a global food challenge. For correct food labelling, the detection and quantification of allergens are necessary. However, novel product formulations and industrial processes produce new scenarios, which require much more technological developments. For this purpose, OMICS technologies, especially proteomics, seemed to be relevant in this context. This review summarises the current knowledge and studies that used proteomics to study food allergens. In the case of the allergenic proteins, a wide variety of isoforms, post-translational modifications and other structural changes during food processing can increase or decrease the allergenicity. Most of the plant-based food allergens are proteins with biological functions involved in storage, structure, and plant defence. The allergenicity of these proteins could be increased by the presence of heavy metals, air pollution, and pesticides. Targeted proteomics like selected/multiple reaction monitoring (SRM/MRM) have been very useful, especially in the case of gluten from wheat, rye and barley, and allergens from lentil, soy, and fruit. Conventional 1D and 2-DE immunoblotting have been further widely used. For animal-based food allergens, the widely used technologies are 1D and 2-DE immunoblotting followed by MALDI-TOF/TOF, and more recently LC-MS/MS, which is becoming useful to assess egg, fish, or milk allergens. The detection and quantification of allergenic proteins using mass spectrometry-based proteomics are promising and would contribute to greater accuracy, therefore improving consumer information.