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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.

Fat, composed mainly of triacylglycerols and phospholipids, and protein, composed of amino acids, constitute major components of meat. Carbohydrate, in the form of glycogen, is present in very low amounts. This article describes the main methodologies available for the analysis of these substances, discusses their advantages and disadvantages, and gives recommendations for the choice of methods.

Alcohol hydydrogenase (ADH) is a key enzyme that influences alcohol metabolism in vivo. Our previous study showed that chicken-derived tripeptide KPC could stabilize ADH in a dose-dependant manner. In this study, possible mechanism underlying how KPC could stabilize ADH was further investigated. Fluorescence quenching data showed that KPC induced a dynamic fluorescence quenching with a quenching rate constant value of 1.074 × 1010 M−1s−1, indicating a conformational change. Circular dichroism further suggested a possible transformation from α-helix (14.03%–13.90%) to random coil (31.98–33.04%) in ADH structure as affected by KPC (5 mmol/L). Molecular docking analysis predicted that KPC may bind to ADH through hydrophobic interaction and hydrogen bonds. Validation of ADH stabilizing activity of fragment peptides and amino acids from KPC implied the vital role of Cys residue to the bio-activity of KPC. These results indicated that KPC may stabilize ADH through peptide-enzyme interactions, and protect ADH against oxidative modification. Besides, a favorable absorption, distribution, metabolism, excretion, and toxicity (ADMET) profile of KPC was obtained using in silico assays. Overall, this study provided a comprehensive understanding on the interaction mechanism between KPC and ADH, and illustrated the potential applicability of KPC as drug or functional food ingredient., This work was supported by the National Natural Science Foundation of China (No. 32101896 and No. 31871746), Key-Area Research and Development Program of Guangdong Province (2021B0707060001), the Self-innovation Research Funding Project of Hanjiang Laboratory (HJL202010B002, HJL202101B001, HJL202101B004,and HJL202101B005), and the Chaozhou Science and Technology Project (2020PT01).

Chicken hydrolysates (CHs) have been reported to protect mice against alcoholic liver injury possibly through oxidative stress reduction. In this study, the antioxidant activity of CHs was studied. Results showed that CHs exhibited significant antioxidant activity (around 600 and 400 μM TEAC/g in ORAC and ABTS assay, respectively) and could resist simulated gastrointestinal digestion. A total of 22 peptides were identified after antioxidant activity-oriented isolation using size-exclusion chromatography and high-performance liquid chromatography. Further in silico analysis and the validation of antioxidant activity revealed that novel peptides (RWGG and YYCQ) exhibited strong antioxidant activity. The most active peptide YYCQ displayed a TEAC value of 3.54 and 4.28 μM TEAC/μM in ORAC and ABTS assay, respectively. These peptides could contribute to reduce oxidative stress and protect against alcohol-induced liver injury. However, further studies understanding the bioactivity of such peptides in vivo are necessary before further applying them as functional food ingredient., This work was supported by the National Natural Science Foundation of China (No. 32101896 and No. 31871746), Key-Area Research and Development Program of Guangdong Province (2021B0707060001), and Self-innovation Research Funding Project of Hanjiang Laboratory (HJL202010B002). Grant AGL2017-89381-R funded by MCIN/ AEI /10.13039/501100011033 by “ERDF A way of making Europe” is acknowledged and grant RYC-2016-19635 (L.M.) funded by MCIN/AEI /10.13039/501100011033 and “ESF Investing in your future” is also acknowledged.

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.

The processing of dry-cured ham results in the generation of small peptides by the action of endogenous enzymes on muscle proteins. Common proteomic workflows involve previous separation techniques based on liquid chromatography which are expensive and time-consuming. In this study, a convenient proteomic approach based on MALDI-ToF is proposed for the first time for the detection of dipeptides in Spanish dry-cured ham. Dipeptides AH, AL, DD, EV, and VF were identified in hams of 18 and 24 months of dry-curing. This work provides insights on the efficiency of a new peptidomic workflow for the short peptide identification from a complex food matrix and permits to evaluate the sample in terms of the presence of taste-related and bioactive dipeptides., Grant AGL2017-89381-R funded by MCIN/ AEI /10.13039/501100011033 by “ERDF A way of making Europe”,is acknowledged. Grant PRE2018-083367 (A.H.) funded by MCIN/AEI /10.13039/501100011033 and “ESF Investing in your future” and grant RYC-2016-19635 (L.M.) funded by MCIN/AEI /10.13039/501100011033 and “ESF Investing in your future” are also acknowledged. The proteomic analysis was performed in the proteomics facility of SCSIE University of Valencia that belongs to Proteored, PRB3 and is supported by grant PT17/0019, of the PE I+D+i 2013-2016, funded by ISCIII and ERDF.

Meat and meat products constitute an important source of nutrients and play vital roles for growth, maintenance and repair of the body. In addition to the high quality of proteins, meat is also regarded as a major resource to produce bioactive peptides. Meat processing industry also produces by-products such as bones, blood and viscera, which could be further used for the production of bioactive compounds. In the physiological analysis, meat bioactive peptides have been reported to exert antioxidant, anti-hypertensive, anti-inflammatory, anti-microbial and antitumoral activities, which endow nutritional and functional value of meat. With the objective to exert the functional effect, the bioavailability should also be considered due to the degradation by digestion enzymes and the absorption process in intestinal mucosa. In this chapter, the general source, the enzymatic hydrolysis, the physiological effects as well as the bioavailability of bioactive peptides in meat are discussed.

A large number of bioactive peptides have been reported with a variety of benefits for human health like angiotensin-converting enzyme inhibition, antioxidant, antiinflammatory, hypoglycemic, or antithrombotic activity, among others. Bioactive peptides are generated through the enzymatic breakdown of proteins either in the food itself by endogenous or microbial peptidases, or in reactors with commercial peptidases. Once consumed, gastrointestinal digestion may also contribute to further generation of bioactive peptides. Endopeptidases are those acting first on proteins followed by the action of exopeptidases on the generated polypeptides and peptides. This chapter is reporting the enzymes and mechanisms involved in the hydrolysis of food proteins for the generation of bioactive peptides.

Microenvironmental factors may influence the antioxidant efficacy of food-derived peptides. This study evaluated the in vitro antioxidant properties of peptides released during the ripening (9 to 24 months of processing) of Spanish dry-cured ham (Biceps femoris muscle) assisted by spectral-chromatographic methodologies. Results indicated that 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) radical-cation (ABTS●+) quenching capacity of peptide extracts significantly increased (P < 0.05) until 24 months whereas peroxyl radical (ROO●) scavenging activity increased slowly and remained with non-significant change (P > 0.05) between 15 and 24 months. However, both ferric reducing antioxidant power (FRAP) and 2,2-diphenyl-1-picrylhydrazyl radical (DPPH●) scavenging ability significantly decreased (P < 0.05) at 24 months. Additionally, morphological traits of peptide extracts suggested that a prolonged ripening enabled the formation/reconstruction of intra-/inter-molecular interactions in dispersion medium. Meta-analysis of chromatographic and spectral fingerprinting proved that the non-conjugated/π-conjugated oligomers mediated by aromatic moieties probably differentiated DPPH● and ABTS●+ antioxidant performance of peptides, showing a potentially altered solvent polarization process., 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. C.L. appreciated the financial support from China Scholarship Council (CSC) through the State Scholarship Fund for Overseas Study (No. 201806760050).

Peptidomics is considered an essential tool for the identification and quantitation of naturally generated peptides present in complex matrices from animal and vegetable origin. These peptides have been generated in natural processes such as fermentation, curing, or maturation, due to the action of endogenous or microbial enzymes, and even, once ingested, from the action of gastrointestinal enzymes during the digestion. The peptides generated have a widespread range of sizes and nonspecific cleavage sites, and certain primary steps such as solid-phase extraction, ultrafiltration, or chromatography are necessary to reduce the complexity of the matrix and avoid interferences to the identification and quantification of the peptides by mass spectrometry approaches. Thus the identification and quantification of naturally generated peptides require and adaptation of the analytical and experimental protocols of previously used proteomics strategies.

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.

Peptides and free amino acids are naturally generated in dry-cured ham as a consequence of proteolysis phenomenon exerted by muscle peptidases. The generation of bioactive peptides in different types of dry-cured ham produced in Spain, Italy and China is reviewed in this manuscript. Major muscle proteins are extensively hydrolysed firstly by endogenous endo-peptidases followed by the successive action of exo-peptidases, mainly, tri- and di-peptidylpeptidases, aminopeptidases and carboxypeptidases. Such proteolysis is very intense and consists of the generation of large amounts of free amino acids and a good number of peptides with different sequences and lengths, some of them exerting relevant bioactivities like angiotensin converting enzyme inhibitory activity, antioxidant activity, di-peptidylpeptidase IV inhibitory activity among other and in vivo antihypertensive, hypoglycemic or anti-inflammatory activity. This manuscript reviews the recent findings showing that dry-cured ham constitutes a good source of natural bioactive peptides that have potential benefit for human health., The research leading to these results received funding from Grant AGL2017-89831-R from the Spanish Ministry of Economy, Industry and Competitivity and FEDER funds The Ramón y Cajal postdoctoral contract to LM is also acknowledged.

There is a wide range of chemicals that may be present in meat as residues either during processing or during cooking and household management. Analytical technologies are constantly being developed and improved, allowing the correct detection and determination of such compounds and contributing to a better meat safety. Some toxic compounds that may be present in meat or meat products are N-nitrosamines as a consequence of nitrite use, polycyclic aromatic hydrocarbons generated from smoking, oxidation of lipids and proteins, and, finally, other substances resulting from the raw materials used in animal production like veterinary drug residues or environmental contaminants. All these are harmful compounds and the available detection analyses are described in this chapter.

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.