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Alcohol-induced liver injury has become a leading risk for human health, however, effective strategies for the prevention or treatment are still lacking. Hence, the present study explored the potential of Musculus senhousei as a source of hepatoprotective peptides against alcoholic liver injury using in vitro, in vivo and in silico methods. Results indicated that Musculus senhousei peptides (MSP, extracted by simulated gastrointestinal digestion of cooked mussel) exhibited notable antioxidant (ABTS and DPPH assays) and alcohol dehydrogenase (ADH) stabilizing activity in vitro. The ingestion of MSP markedly alleviated alcohol-induced liver injury in mice, as indicated by the decrease of serum transaminases (AST and ALT). In line with in vitro assays, significantly increased hepatic ADH activity and activated antioxidative defense system (GSH, SOD, GSH-Px and CAT) were observed, whereas the oxidative stress (MDA) was decreased. Peptidomic analysis revealed over 6000 peptides with favorable amino acid compositions, and a total of 20 potentially novel peptides with bioactivity and bioavailability were excavated among 746 of the most influential peptides using an in silico strategy. Peptides (i.e. WLPMKL, WLWLPA, RLC and RCL) were further synthesized and validated in vitro to be bioactive. These findings suggest that Musculus senhousei can be an ideal source of bioactive peptides for the prevention of alcoholic liver injury., This work was supported by the Key-Area Research and Development Program of Guangdong Province (2022B0202030001 and 2021B0707060001), the National Natural Science Foundation of China (No. 32101896) and Self-innovation Research Funding Project of Hanjiang Laboratory (HJL202010B002).

Bile acids are involved in the modulation of various metabolic processes facilitating the biliary excretion of endogenous and exogenous cholesterol. The objective of this study was to determine the glycocholic acid binding capacity (BC) of chicken blood hydrolysates using an optimized RP-HPLC methodology. Samples were hydrolysed using a combination of five different enzymes. Alcalase and Protamex hydrolysates presented the highest BC, with mean values of 20.09% and 20.61%, respectively. Subsequently, both hydrolysates were ultrafiltered to obtain fractions >10 kDa, between 10 and 3 kDa, and 10 kDa. Finally, the protein fragments (MW > 10 kDa) potentially responsible for BC were identified by LC-MS/MS. The results confirmed the relation of BC with the molecular weight of the peptides generated, suggesting that certain protein fragments generated from chicken blood could contribute to a positive impact on health by interfering with cholesterol metabolism., Grant PID2020-119684RB-I00 funded by MCIN/AEI/10.13039/501100011033 is acknowledged. Grant GRISOLIAP/2020/021 de la Consellería de Innovació, Universitats, Ciència i Societat Digital de la Generalitat Valenciana (GCA) is also acknowledged. The proteomic analysis was performed in the proteomics facility of SCSIE University of Valencia belonging to Proteored.

Sweet dipeptide Ala-Ala (AA) could be one of the most abundant dipeptides naturally generated in meat products due to the high occurrence of its sequence all along endogenous proteins, which means it could play a key role in dry-cured ham flavour development and bioactivity. In this study, a mass spectrometry in tandem methodology was optimised to quantitate the dipeptide AA in dry-cured ham manufactured under different processing conditions. Dipeptide values reached 230 µg/g after 12-month of ripening, but statistically insignificant differences were observed with salt reduction. Regarding its antihypertensive activity, an IC50 value of 110.824 µM was determined from the in vitro inhibition of angiotensin-I converting (ACE-I) enzyme, and the oral administration of 1 mg of AA per kg of body weight showed a significant reduction of the systolic blood pressure (SBP) in spontaneous hypertensive rats (SHR). This study elucidates the importance of AA dipeptide and its potential role in cardiovascular health after dry-cured ham consumption., Grant AGL2017-89381-R funded by MCIN/ AEI /https://doi.org/10.13039/501100011033 by “ERDF A way of making Europe” is acknowledged. Grant PRE2018-083367 (A.H.) funded by MCIN/AEI /https://doi.org/10.13039/501100011033 and “ESF Investing in your future” and grant RYC-2016–19635 (L.M.) funded by MCIN/AEI /https://doi.org/10.13039/501100011033 and “ESF Investing in your future” are also acknowledged. Arihara funding KAKENHI (21H02348) from Japan Society for the Promotion of Science is also acknowledged.

Refers to: Chuqiao Xiao, Mouming Zhao, Feibai Zhou, Marta Gallego, Jie Gao, Fidel Toldrá, Leticia Mora. Isolation and identification of alcohol dehydrogenase stabilizing peptides from Alcalase digested chicken breast hydrolysates. Journal of Functional Foods 64:103617 (2020), Bioactive peptides have attracted extensive attention worldwide as natural alternatives to promote human health and wellness. Previous studies have shown that chicken hydrolysates could enhance alcohol dehydrogenase, and subsequently they facilitate alcohol metabolism and ameliorate alcohol-induced liver injury. The data presented in this article support the accompanying research article “Isolation and identification of alcohol dehydrogenase stabilizing peptides from Alcalase digested chicken breast hydrolysates”. Present article details all 82 peptides identified from the most active fractions of chicken hydrolysates, and 154 peptides from in silico digestion of the 82 identified peptides, together with the prediction of their potential bioactivity and applicability using several in silico assays., This work was supported by Grant AGL2017-89381-R and FEDER funds from the Spanish Ministry of Economy, Industry and Competitiveness, the National Natural Science Foundation of China (No. 31701539 and No.31871746) and the Natural Science Foundation of Guangdong Province (No. 2017A030313127). We also thank Ramón y Cajal postdoctoral contract by L.M. and the China Scholarship Council (CSC) research program for providing funding for C. X.

Large amounts of meat by- and co-products are generated during slaughtering and meat processing, and require rational management of these products for an ecological disposal. Efficient solutions are very important for sustainability and innovative developments create high added-value from meat by-products with the least environmental impact, handling and disposal costs, in its transition to bioeconomy. Some proteins have relevant technological uses for gelation, foaming and emulsification while protein hydrolyzates may contribute to a better digestibility and palatability. Protein hydrolysis generate added-value products such as bioactive peptides with relevant physiological effects of interest for applications in the food, pet food, pharmaceutical and cosmetics industry. Inedible fats are increasingly used as raw material for the generation of biodiesel. Other applications are focused on the development of new biodegradable plastics that can constitute an alternative to petroleum-based plastics. This manuscript presents the latest developments for adding value to meat by- and co-products and discusses opportunities for making meat production and processing more sustainable., Grant from AGL2017-89831-R from the Spanish Ministry of Economy, Industry and Competitivity and FEDER funds.

To investigate the oxidative effect of CPF on chicken breast proteins, peptidomics and proteomics analysis were used. For this, chicken breast samples were exposed to CPF and subjected to simulated gastrointestinal digestion. The identification of oxidized peptides from digested and undigested proteins were performed by LC MS/MS (nanoESI qQTOF). Prior to mass analyses undigested proteins were trypsinated. Data were analysed using MASCOT and ProteinPilot v 4.5 software. In this study, 90 and 107 oxidized peptides from digested proteins of control and exposed samples were identified, respectively. These peptides corresponding to 12 oxidized proteins. Meanwhile, 260 and 324 oxidized peptides from undigested proteins (control and exposed samples) were identified, which corresponding to 19 and 17 proteins, respectively. Collagen was protein more susceptible to oxidation promoted by chlorpyrifos in digested and undigested proteins. Identification of these oxidized proteins from simulated digestion provides an important insight about the impact of substances like certain veterinary drugs at trace concentrations on the nutritional value of chicken breast meat., Grant AGL2017-89381-R and FEDER funds from the Spanish Ministry of Economy, Industry and Competitiveness, and Ramón y Cajal postdoctoral contract by L.M. are acknowledged. Also COLCIENCIAS and University of Cartagena for financial support (2019 and 2020) to the project Code 1107-711-50102 are acknowledged.

The present study aimed to investigate the effect of cooking and simulated gastrointestinal digestion on the antioxidant and alcohol dehydrogenase (ADH) stabilization activity of peptides extracted from chicken breast muscle. Results showed that cooking would not affect peptide bioactivity, whereas further digestion using gastrointestinal enzymes could lead to significant changes, producing an increase in ORAC (112.5 to 682.0 uM TE/g) and ABTS radical scavenging activities (164.0 to 848.9 uM TE/g), whereas a decrease in DPPH radical scavenging (from 36.1% to 4.4%), ferric-reducing power (OD 700 from 0.50 to 0.15) and ADH stabilization activities (from 44.1% to 20.5%) was observed. The peptidomic analysis resulted in the identification and relative quantitation of 777 peptides from 76 different parent proteins and evidenced that peptides derived from titin and collagen were mainly responsible for the differences detected in the peptide profile. The decrease of DPPH radical scavenging, ferric reducing power, and ADH stabilization activity may result from the release of inactive peptides containing oxidized residues, mainly from collagen, leading to the loss of efficacy of active sequences. The results confirmed the importance of collagen derived peptides on the antioxidant and ADH stabilization activity observed in chicken breast as well as the negative impact of oxidation on the bioactivity of generated peptides after simulated gastrointestinal digestion. Nevertheless, further work would be needed to confirm the peptide sequences responsible for the observed bioactivity., This work was supported by Grant AGL2017-89381-R and FEDER funds from the Spanish Ministry of Economy, Industry and Competitiveness, and the National Natural Science Foundation of China (No. 31701539 and No.31871746), and the Natural Science Foundation of Guangdong Province (No. 2017A030313127). Ramón y Cajal postdoctoral contract by LM and the China Scholarship Council (CSC) research program for C. X. are also acknowledged.

This manuscript is reviewing the presence of substances of safety concern that may be generated in different types of meat products. Such substances include N-nitrosamines that can be generated under certain conditions when using nitrite as preservative, the polycyclic aromatic hydrocarbons generated as a consequence of particular smoking processes, heterocyclic aromatic amines generated under particular cooking conditions, compounds released from the oxidation of lipids and proteins, Maillard reaction products like acrylamide and carboxymethyl lysine, and amines that can be generated and accumulated in fermented meats. These hazardous compounds, their mechanisms of generation, risks for health and ways of preventing its presence in meat products are briefly described in this review., Grants AGL2017-89831-R, AGL2015-64673-R and FEDER funds from the Spanish Ministry of Economy, Industry and Competitiveness are acknowledged. Ramón y Cajal postdoctoral contract to LM is also acknowledged.

Myofibrillar proteins are extensively degraded by muscle endo- and exopeptidases during the ageing of meat and the processing of meat products. One of the most studied products is dry-cured ham. This degradation implies changes in the product in terms of texture (mainly due to calpains and cathepsins endopeptidases) and flavour (due to the action of exopeptidases) and defines its final quality. During the last decade, naturally generated peptides from the myofibrillar proteins titin, myosin light chain, troponin T, LIM domain-binding protein 3, and actin have been identified using peptidomic approaches, also showing the potential to act as bioactives in the human body when ingested. In this study, tandem mass spectrometry has been used for the identification of the peptides generated during the proteolysis of myosin heavy chain protein after 9 months of Spanish dry-cured ham processing. The size, sequence, and properties of some of the peptides showed their potential to act as bioactives., Grant AGL2014-57367-R and FEDER funds from the Spanish Ministry of Economy, Industry and Competitiveness are acknowledged. Ramón y Cajal postdoctoral contract to LM is also acknowledged.

During the last decade, the use of integrated ‘omics’ including genomics, transcriptomics, metabolomics and proteomics has provided a better knowledge of food systems. In fact, technical improvements achieved in mass spectrometry instruments together with the last developments of bioinformatics tools and hardware have allowed proteomics to be the method of choice for food control through the identification of quality biomarkers and the study of the proteome expression data. In this context, modern comparative proteomics is the basis for establishing quantitative differences in the expressed proteome of a certain sample by comparison with a reference through the relative and absolute quantification of proteins and peptides., Grant AGL2014-57367-R and FEDER funds from the Spanish Ministry of Economy, Industry and Competitiveness are acknowledged. Juan de la Cierva de Incorporación postdoctoral contract to LM is also acknowledged.

Antioxidant peptides positively regulate oxidative stress in the human body as well as delay, retard or prevent protein and lipid oxidation in food products. Spanish dry-cured ham has been reported as a good source of bioactive peptides, being SNAAC the most active antioxidant peptide identified to date. In this work, the stability of this peptide against in vitro digestion, heat treatments and different salt concentrations was evaluated using three methods for measuring antioxidant activity: β-carotene bleaching assay, ABTS radical scavenging capacity and ORAC assay. The results evidenced a marked decrease in the antioxidant activity of SNAAC after gastrointestinal digestion, and the MALDI-ToF MS analysis revealed the degradation of the peptide after the process, the generation of the fragment SNAA and the presence of a peptide dimer throughout the in vitro digestion. On the other hand, the peptide SNAAC showed good heat stability after exposure to different temperatures (50 °C, 72 °C, and 90 °C), but its antioxidant activity evaluated by ORAC assay decreased substantially when exposed to 100 °C as compared with the control at 37 °C. SNAAC remained stable in the presence of salt at concentrations ranging from 0 to 8% NaCl as well as it was able to inhibit about 40% of lipid oxidation in an emulsion system. These results reported the stability of the antioxidant peptide SNAAC to several conditions used in meat industry for the processing of dry-cured hams and ham-derived products and its effectiveness to partially prevent the lipid oxidation in these products. However, some strategies would be needed in order to increase the stability of the peptide during gastrointestinal digestion and thus improve its bioavailability to be used as functional food ingredient., Emerging Research Group Grant from Generalitat Valenciana in Spain (GV/2015/138) and Juan de la Cierva postdoctoral contract to LM are acknowledged. Grant Agreement 614281 (HIGHVALFOOD) and contract to MG are also acknowledged. The proteomic analysis was performed in the proteomics facility of SCSIE University of Valencia that belongs to ProteoRed, PRB2-ISCIII, (IPT13/0001 - ISCIII-SGEFI/FEDER).

The effect of a beef meat coating prepared using cuttlefish skin gelatin with henna aqueous extract (HAE) as natural preservative was studied during chilled storage of meat at 1, 3, 6 and 8 days. The combined coating increased the shelf-life of meat by decreasing the total and psychrophilic vial bacteria counts at the end of storage. In addition, the lipid oxidation of meat decreased during the period of storage in gelatin-HAE coated samples measured using the thiobarbituric acid reactive substances test. Furthermore, coating significantly preserved color properties in comparison with uncoated samples. According to free amino acid contents, coating decreased the rate of proteolysis process, whereas it was faster in uncoated samples. Thus, the gelatin coatings offer an excellent protection to avoid meat deterioration, which was significantly improved by the addition of HAE to the gelatin gel., The Ministry of Higher Education and Scientific Research of Tunisia is acknowledged. The research leading to these results has also received funding from the Spanish Ministry of Economy and Competitiveness, AGL2014-57367-R, and FEDER funds. Juan de la Cierva de Incorporación postdoctoral contract (L.M.) funded by the Spanish Ministry of Economy and Competitiveness is fully acknowledged.

Sardinelle protein hydrolysate (SPH), prepared by treatment with Bacillus subtilis A26 proteases, was found to exhibit antibacterial, antioxidant and ACE-inhibitory activities. SPH, with a degree of hydrolysis of 4%, was fractionated by size exclusion chromatography on a Sephadex G-25 into five major fractions (F1–F5). F2, which exhibited the highest antibacterial and ACE-inhibitory activities, and F4, which exhibited the highest antibacterial and antioxidant activities, were further fractionated by reverse phase-high performance liquid chromatography (RP-HPLC) and then analysed using nano-ESI-LC-MS/MS to identify the sequences of peptides. Eight peptides were identified in the sub-fraction F2-A, nine peptides in the sub-fraction F4-B, and 45 peptides in F4-C. Identified peptides were found to share sequences with previously described bioactive peptides based on Biopep database. The results of this study suggest that SPH is a good source of natural bioactive peptides. Hence, it can be used as a potential ingredient in nutraceutical field., This work was funded by the Ministry of Higher Education and Scientific Research-Tunisia. Grant AGL2014-57367-R from MINECO (Spain) and FEDER funds and JAEDOC-CSIC postdoctoral contract of L.M. cofounded by the European Social Found are acknowledged. LC-MS/MS analysis was carried out in the SCSIE University of Valencia Proteomics Unit (Spain), a member of ISCIII ProteoRed Proteomics Platform.

The effect of ultrasound (US) pre-treatment on the evolution of Maillard reaction (MR), induced between low molecular weight (LMW) peptides and sucrose, was studied. LMW peptides (, This work was funded by the Ministry of Higher Education and Scientific Research, Tunisia. Emerging Research Group Grant from Generalitat Valenciana in Spain (GV/2015/138) and JAEDOC-CSIC postdoctoral contract of L.M. cofounded by the European Social Found are acknowledged.

A large number of peptides are generated during the processing of dry-cured ham that can be affected by post-translational modifications (PTM). One of the most studied PTMs is the oxidation of susceptible residues but other modifications such as deamidation have been scarcely reported in the literature. This work has been focused on the impact of deamidation in those peptides generated in 12-months dry-cured hams. The results obtained in Biceps femoris and Semimembranosus muscles showed that 52% and 48% of the identified peptides, respectively, were affected by PTMs, with a total of 277 and 282 sequences showing deamidation in both muscles, respectively. It appears that deamidation is not influenced by the type of muscle but is probably favored by characteristic processing conditions like temperature, pH, and salting of hams. The knowledge of the affected sequences provides novel information for a better characterisation of proteolysis phenomena during the processing of dry-cured ham., The research leading to these results has received funding from the Spanish Ministry of Economy, Industry and Competitiveness, AGL2014-57367-R and FEDER funds. FPI Scholarship to MC and Juan de la Cierva de Incorporación postdoctoral contract to LM are acknowledged.

Background: The final characteristics of processed meats depend on many factors but one of the most important is the intense proteolysis occurred in muscle proteins due to the action of endogenous enzymes in dry-cured ham, and also microbial peptidases in the case of dry-fermented meats, that not only affects taste and flavour but also the generation of bioactive peptides. Scope and approach: In this review main difficulties in the identification of bioactive peptides in processed meats have been described. This study highlights the novel strategies used during the last years to identify naturally generated peptides, and emphasises the need of robust quantitative methodologies for the adequate characterisation of their bioavailability. In fact, the most common and well established quantitation approaches using proteomics are not adapted for peptidomics analysis, so alternative strategies need to be considered. Key findings and conclusions: The progress in the identification and characterisation of the activity of natural bioactive peptides is highly dependent on modern instruments and bioinformatics tools as well as updated protein databases. In fact, the use of in silico approaches and proteomics can be complementary tools in the identification of peptides from meat protein sources as the empirical experimental design can be simplified by using bioinformatics for computer simulation in most of the steps. Finally, Multiple Reaction Monitoring mass spectrometry methodology previously used in the quantitation of therapeutic peptides and biomarkers arises as a powerful tool for absolute quantitation or semi-quantitation of bioactive peptides., The research leading to these results received funding from the European Union 7th Framework Programme (FP7/2007–2013) under Grant Agreement 312090 (BACCHUS). This publication reflects only the author views and the Community is not liable for any use made of the information contained therein. Grant AGL2014-57367-R from MINECO and FEDER funds and the Juan de la Cierva postdoctoral contract to LM are acknowledged. The proteomic analysis was performed in the proteomics facility of SCSIE University of Valencia that belongs to ProteoRed, PRB2-ISCIII, (IPT13/0001 - ISCIII-SGEFI/FEDER).

This study is focused on the characterization of the proteolysis occurred during the processing of Pastırma, a traditional Turkish dry-cured meat product, which is responsible for its final characteristics. Thus, the evaluation of naturally generated free amino acids and peptides present at 0, 2, 5, 10, and 21 days of processing and the bioactivity of peptide fractions have been approached. Peptides were examined by MALDI-TOF and results showed differences in the amount of generated peptides at different times of processing, and a total of 29 peptides were newly generated at Day 21 in comparison with Day 2 during processing. The water soluble fraction of Pastırma at the end of the curing period (Day 21) was also analyzed by size-exclusion chromatography and some of the collected fractions demonstrated strong ACE-inhibitory and antioxidant activities. In fact, Pastırma showed an ACE inhibitory activity higher than 86% from 220 to 270 mL corresponding to molecular masses between 900 and 1500 Da, and also a DPPH radical-scavenging activity above 60% at 250 to 300 mL corresponding to molecular masses between 700 and 2000 Da. Thus, Pastırma represents a good source of natural ACE-inhibitory and antioxidant peptides which might be due to the proteolysis occurred by endogenous enzymes and the contribution of the çemen paste used in production., Grant AGL2014-57367-R from MINECO (Spain) and FEDER funds and JAEDOC-CSIC postdoctoral contract of L.M. cofunded by European Social Funds are acknowledged. The research fellowship grant provided by Erasmus + KA1 Student Mobility Programme for Higher Education for the author Ebru Deniz is also gratefully acknowledged.

[EN] Simultaneous brine thawing/salting process was applied as an alternative to traditional pile salting process using 51 frozen Iberian hams. The effect of this type of salting process on endogenous enzyme activity and sensory quality of Iberian dry-cured hams was analysed. The frozen hams were simultaneously thawed and salted with saturated brine, with and without vacuum pulses, and were compared to hams thawed under refrigeration and traditionally salted. The peptidase and lipase activities were measured at the end of salting and post-salting stages. The activity of cathepsin B+L was reduced in the two brine salted batches while few differences among batches were observed for the other peptidases. Several lipase activities were significantly reduced in the two brine salted batches. The brine thawed processing affected the free fatty acid content at the different stages although the differences were more appreciated at the beginning of the process and no differences were observed at the end. The long ripening time makes these differences negligible and the consumer did not appreciate any differences between the sensory quality of Iberian brine/thawed hams and traditional Iberian thawed pile salted hams. (C) 2011 Elsevier Ltd. All rights reserved., Financial support from PETRI by the Ministry of Science and Innovation (PTR-1995-0754-OP-03) is fully acknowledged. Work was carried out under the Unidad Asociada IIAD (UPV) - IATA (CSIC) framework. The authors are grateful to M. Lozano and MI. Nadal for technical assistance.

[EN] Meat and meat products are generally recognised as good sources of high biological-value proteins, group B vitamins, minerals and trace elements as well as some other bioactive compounds. However, the image to consumers is relatively negative due to their involvement in prevalent diseases of Western societies like cardiovascular diseases, cancer and obesity. Recent innovations in the meat industry are addressed towards the production of healthier meats and processed meats. The strategies are based on either reducing the content of unhealthy substances (i.e. less added sodium chloride, less nitrate and nitrite) or improving the content of substances with healthy benefits (i.e. natural antioxidants, omega-3 fatty acids, probiotics and bioactive peptides). © 2011 Elsevier Ltd., Grant AGL2010-16305 from the Spanish Ministry of Science and Innovation (Madrid, Spain) and FEDER funds and grant from Vaquero Foundation for RþD on Pork Meat (Madrid, Spain) are acknowledged. Work prepared within the Unidad Asociada IAD (UPV)-IATA (CSIC) framework.

[EN] The use of dielectric properties at low frequencies to estimate the progress of pork meat (Longissimus dorsi) ageing was evaluated. Dielectric measurements were perfomed at 140 Hz, 1 kHz and 300 kHz in perpendicular to the long axis of the meat muscle fibers at 12, 24,48 and 168 h post-mortem. Principal Component Analysis (PCA) was used to describe the relationships between meat physical/biochemical parameters and dielectric parameters of pork meat. Good correlations were found between the ageing indexes (Al(sigma) and Al(epsilon')) calculated from dielectric properties and some parameters of texture such as hardness and chewiness. Moreover, both indexes correlated well with free amino acids content, and with K value. The high degree of correlation confirms the viability of using the ageing indexes obtained from dielectric measurements to evaluate the degree of ageing of pork meat, giving information about some important eating quality parameters. (C) 2011 Elsevier Ltd. All rights reserved., Grant from Agroalimed (Conselleria de Agricultura, Pesca y Alimentacion, Valencia, Spain) and FPU grant to MC from Ministry of Science and Innovation (Madrid, Spain) are fully acknowledged. Work prepared within the Unidad Asociada IAD (UPV)-IATA (CSIC) framework.

[EN] Dielectric measurements of different standard solutions (nucleotides, nucleosides, lactic acid and myoglobin) were assayed simulating the concentrations of these substances in early postmortem meat. These assays were performed for considering the potential use of dielectric spectra for the quality control of meat. Good correlations among solutions of Adenosine Triphosphate (ATP), Inosine Monophosphate (IMP) and lactic acid with loss factor at punctual frequencies (0.5, 0.915 and 1 GHz) were found. The other assayed substances did not present a marked effect over the electromagnetic spectra. Good correlations of dielectric properties with IMP and lactic acid content of real pork meat samples were also found at 0.5 GHz. This work is presenting prospective data of dielectric spectra for certain key biochemical markers in order to consider its potential application as a non-destructive control sensor for the prediction of pork meat quality. (C) 2010 Elsevier Ltd. All rights reserved., Grant from Agroalimed (Conselleria de Agricultura, Pesca y Alimentacion, Valencia, Spain) and FPU grant to M.C. from Ministry of Science and Innovation (Madrid, Spain) are fully acknowledged. Work prepared within the Unidad Asociada IAD (UPV)-IATA (CSIC) framework.

Dry-cured ham is a traditional product with a strong presence in markets in the Mediterranean area. It is very popular with European consumers and is of enormous economic importance for the meat industry in the Mediterranean area. Although the great palatability of ham largely outweighs other considerations, aspects relating to health and wellbeing are increasingly important factors in consumer decisions. The potential role of ham in a context of healthy nutrition has not been clearly elucidated, especially considering that origins and production methods of dry-cured hams can induce differences in composition. The object of this review was on the one hand to provide an analysis of the components of dry-cured ham and their role in a healthy diet, and on the other hand to suggest possible strategies for improving its nutritional composition. © 2009 Elsevier Ltd. All rights reserved.