{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,21]],"date-time":"2026-01-21T18:13:04Z","timestamp":1769019184004,"version":"3.49.0"},"reference-count":29,"publisher":"MDPI AG","issue":"22","license":[{"start":{"date-parts":[[2020,11,19]],"date-time":"2020-11-19T00:00:00Z","timestamp":1605744000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Seventh Framework Programme","award":["FP726719"],"award-info":[{"award-number":["FP726719"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Collagen antioxidant peptides are being widely studied. However, no research has paid attention to biological parameters such as the age and anatomy of collagen-rich tissues, which can determine a change in tissue structure and composition, and then in bioactivity. Moreover, only few research works have studied and assessed peptides antioxidant activity on the food matrix. This work aimed to investigate the effect of bovine\u2019s bone age and anatomy, and of six different enzymes, on the antioxidant activity of collagen peptides. Collagen was extracted from young and old bovine femur and tibia; six different enzymes were used for peptides\u2019 release. The redox potential, the quenching of stable free radicals, and the antioxidant capacity on bovine meat lipids and proteins was evaluated, under heating from ambient temperature to 80 \u00b0C. Age and anatomy showed a significant effect; the influence of anatomy becomes most important with age. Each enzyme\u2019s effectiveness toward age and anatomy was not the same. The greatest amount of peptides was released from young bones\u2019 collagen hydrolysed with papain. The antioxidant activity was higher at higher temperatures, except for meat proteins. Assessing the effect of age and anatomy of collagen-rich tissues can promote a better application of collagen bioactive peptides.<\/jats:p>","DOI":"10.3390\/molecules25225422","type":"journal-article","created":{"date-parts":[[2020,11,19]],"date-time":"2020-11-19T10:46:26Z","timestamp":1605782786000},"page":"5422","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Redox Potential and Antioxidant Capacity of Bovine Bone Collagen Peptides towards Stable Free Radicals, and Bovine Meat Lipids and Proteins. Effect of Animal Age, Bone Anatomy and Proteases\u2014A Step Forward towards Collagen-Rich Tissue Valorisation"],"prefix":"10.3390","volume":"25","author":[{"given":"Laurent","family":"Aubry","sequence":"first","affiliation":[{"name":"INRAE, QuaPA, 63122 Saint-G\u00e8nes-Champanelle, France"}]},{"given":"Claude","family":"De-Oliveira-Ferreira","sequence":"additional","affiliation":[{"name":"INRAE, QuaPA, 63122 Saint-G\u00e8nes-Champanelle, France"}]},{"given":"V\u00e9ronique","family":"Sant\u00e9-Lhoutellier","sequence":"additional","affiliation":[{"name":"INRAE, QuaPA, 63122 Saint-G\u00e8nes-Champanelle, France"}]},{"given":"Vincenza","family":"Ferraro","sequence":"additional","affiliation":[{"name":"INRAE, QuaPA, 63122 Saint-G\u00e8nes-Champanelle, France"}]}],"member":"1968","published-online":{"date-parts":[[2020,11,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1813","DOI":"10.1016\/j.foodhyd.2011.02.007","article-title":"Functional and bioactive properties of collagen and gelatin from alternative sources: A Review","volume":"25","author":"Monteiro","year":"2011","journal-title":"Food Hydrocoll."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1146\/annurev-food-031414-111800","article-title":"Collagen and Gelatin","volume":"6","author":"Liu","year":"2015","journal-title":"Annu. 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