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-A Step Forward towards Collagen-Rich Tissue Valorisation.

Laurent Aubry,Claude De-Oliveira-Ferreira,Véronique Santé-Lhoutellier,Vincenza Ferraro

doi:10.3390/molecules25225422

Laurent Aubry, Claude De-Oliveira-Ferreira + Show 2 more

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https://doi.org/10.3390/molecules25225422

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Abstract

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’s 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’ 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 °C. Age and anatomy showed a significant effect; the influence of anatomy becomes most important with age. Each enzyme’s effectiveness toward age and anatomy was not the same. The greatest amount of peptides was released from young bones’ 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.

Highlights

Collagen peptides from animal tissues such as skin, tendons, cartilages, bone, etc., have been screened worldwide for numerous biological activities [1,2,3]
The amount of collagen peptides varied according to the enzyme used for hydrolysis, and with the bone’s age and anatomy
For the 3000 Da cut-off, the greatest hydrolytic effect was noticed for papain on young bones (Figure 1)

Summary

Introduction

Collagen peptides from animal tissues such as skin, tendons, cartilages, bone, etc., have been screened worldwide for numerous biological activities [1,2,3]. Great potential has been shown and in several fields such as food, nutrition, health, cosmetics, materials and biomaterials, sensors, textiles. While several enzymes and hydrolysis parameters have been tested and optimised, none of the research reported in literature has assessed the effect of some important biological parameters, such as the anatomy of collagen-rich tissues and the age of the animal (or marine) species, on the bioactivity of the collagen peptides. Very few studies have been carried out to assess the potential of bioactive peptides on the food matrix, and those mainly focus on peptides from pork meat and bovine haemoglobin [5]

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