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"This document is the unedited Author's version of a Submitted Work that was subsequently accepted for publication in Journal of Agricultural and Food Chemistry, copyright © American Chemical Society after peer review. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.jafc.9b08297", [EN] There is a wide variety of peptides released from food proteins that are able to exert a relevant benefit for human health, such as angiotensin-converting enzyme inhibition, antioxidant, anti-inflammatory, hypoglucemic, or antithrombotic activity, among others. This manuscript is reviewing the recent advances on enzymatic mechanisms for the hydrolysis of proteins from foods of animal origin, including the types of enzymes and mechanisms of action involved, the strategies followed for the isolation and identification of bioactive peptides through advanced proteomic tools, and the assessment of bioactivity and its beneficial effects. Specific applications in fermented and/or ripened foods where a significant number of bioactive peptides have been reported with relevant in vivo physiological effects on laboratory rats and humans as well as the hydrolysis of animal food proteins for the production of bioactive peptides are also reviewed.

"This document is the unedited Author's version of a Submitted Work that was subsequently accepted for publication in Journal of Agricultural and Food Chemistry, copyright © American Chemical Society after peer review. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.jafc.9b08297", [EN] There is a wide variety of peptides released from food proteins that are able to exert a relevant benefit for human health, such as angiotensin-converting enzyme inhibition, antioxidant, anti-inflammatory, hypoglucemic, or antithrombotic activity, among others. This manuscript is reviewing the recent advances on enzymatic mechanisms for the hydrolysis of proteins from foods of animal origin, including the types of enzymes and mechanisms of action involved, the strategies followed for the isolation and identification of bioactive peptides through advanced proteomic tools, and the assessment of bioactivity and its beneficial effects. Specific applications in fermented and/or ripened foods where a significant number of bioactive peptides have been reported with relevant in vivo physiological effects on laboratory rats and humans as well as the hydrolysis of animal food proteins for the production of bioactive peptides are also reviewed.

There is a wide variety of peptides released from food proteins that are able to exert a relevant benefit for human health, such as angiotensin-converting enzyme inhibition, antioxidant, anti-inflammatory, hypoglucemic, or antithrombotic activity, among others. This manuscript is reviewing the recent advances on enzymatic mechanisms for the hydrolysis of proteins from foods of animal origin, including the types of enzymes and mechanisms of action involved, the strategies followed for the isolation and identification of bioactive peptides through advanced proteomic tools, and the assessment of bioactivity and its beneficial effects. Specific applications in fermented and/or ripened foods where a significant number of bioactive peptides have been reported with relevant in vivo physiological effects on laboratory rats and humans as well as the hydrolysis of animal food proteins for the production of bioactive peptides are also reviewed.

"This document is the unedited Author s version of a Submitted Work that was subsequently accepted for publication in Journal of Agricultural and Food Chemistry, copyright © American Chemical Society after peer review. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.jafc.8b05888", [EN] The interest in using food byproducts as a source of bioactive peptides has increased significantly in the recent years. The goal of this work was to determine the presence and stability of peptides showing angiotensin I-converting enzyme (ACE-I), endothelin-converting enzyme (ECE), dipeptidyl peptidase-IV (DPP-IV), and platelet-activating factor-acetylhydrolase (PAF-AH) inhibitory activity derived from dry-cured ham bones, which could exert cardiovascular health benefits. ACE-I and DPP-IV inhibitory peptides were stable against heating typically used in Mediterranean household cooking methods and also to in vitro digestion. PAF-AH inhibitory activity significantly increased following simulated gastrointestinal digestion whereas ECE inhibitory significantly decreased (P < 0.05). The mass spectrometry analysis revealed a notable degradation of hemoglobin-derived peptides after simulated digestion, and the release of a large number of dipeptides that may have contributed to the observed bioactivities. These results suggest that natural peptides from Spanish dry-cured ham bones could contribute to a positive impact on cardiovascular health.

"This document is the unedited Author s version of a Submitted Work that was subsequently accepted for publication in Journal of Agricultural and Food Chemistry, copyright © American Chemical Society after peer review. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.jafc.8b05888", [EN] The interest in using food byproducts as a source of bioactive peptides has increased significantly in the recent years. The goal of this work was to determine the presence and stability of peptides showing angiotensin I-converting enzyme (ACE-I), endothelin-converting enzyme (ECE), dipeptidyl peptidase-IV (DPP-IV), and platelet-activating factor-acetylhydrolase (PAF-AH) inhibitory activity derived from dry-cured ham bones, which could exert cardiovascular health benefits. ACE-I and DPP-IV inhibitory peptides were stable against heating typically used in Mediterranean household cooking methods and also to in vitro digestion. PAF-AH inhibitory activity significantly increased following simulated gastrointestinal digestion whereas ECE inhibitory significantly decreased (P < 0.05). The mass spectrometry analysis revealed a notable degradation of hemoglobin-derived peptides after simulated digestion, and the release of a large number of dipeptides that may have contributed to the observed bioactivities. These results suggest that natural peptides from Spanish dry-cured ham bones could contribute to a positive impact on cardiovascular health.

[EN] One of the main biochemical changes that take place during the processing of dry-cured ham is the degradation of the muscle protein fraction, mainly due to the action of muscle enzymes. In the present study, the isolation and tentative identification of 137 fragments from myosin light chain 1 (MLC 1), together with 88 fragments originated from myosin light chain 2 (MLC 2), have been achieved for the first time in Spanish dry-cured ham, proving the intense proteolysis experienced by myofibrillar proteins after dry-cured processing. This study was carried out by use of proteomic technology for peptide identification, and the possible enzymes contributing to the degradation of these proteins were also further discussed.

[EN] One of the main biochemical changes that take place during the processing of dry-cured ham is the degradation of the muscle protein fraction, mainly due to the action of muscle enzymes. In the present study, the isolation and tentative identification of 137 fragments from myosin light chain 1 (MLC 1), together with 88 fragments originated from myosin light chain 2 (MLC 2), have been achieved for the first time in Spanish dry-cured ham, proving the intense proteolysis experienced by myofibrillar proteins after dry-cured processing. This study was carried out by use of proteomic technology for peptide identification, and the possible enzymes contributing to the degradation of these proteins were also further discussed.