Abstract

Antioxidant peptides are gradually being accepted as food ingredients, supplemented in functional food and nutraceuticals, to positively regulate oxidative stress in the human body against lipid and protein oxidation. Meat muscle and meat by-products are rich sources of proteins and can be regarded as good materials for the production of bioactive peptides by use of enzymatic hydrolysis or direct solvent extraction. In recent years, there has been a growing number of studies conducted to characterize antioxidant peptides or hydrolysates derived from meat muscle and by-products as well as processed meat products, including dry-cured hams. Antioxidant peptides obtained from animal sources could exert not only nutritional value but also bioavailability to benefit human health. This paper reviews the antioxidant peptides or protein hydrolysates identified in muscle protein and by-products. We focus on the procedure for the generation of peptides with antioxidant capacity including the acquisition of crude peptides, the assessment of antioxidant activity, and the purification and identification of the active fraction. It remains critical to perform validation experiments with a cell model, animal model or clinical trial to eliminate safety concerns before final application in the food system. In addition, some of the common characteristics on structure-activity relationship are also reviewed based on the identified antioxidant peptides.

Highlights

  • Reactive oxygen species (ROS) including OH, O2 −, HO2, and ROO, and reactive nitrogen species (RNS) including NO and ONOO, are well-known as free radicals produced by endogenous oxidation-reduction (REDOX) reactions in eukaryotes [1]

  • The endogenous enzymes of superoxide dismutase (SOD), catalase, peroxidases, and thioredoxin are responsible for scavenging free radicals and natural antioxidants and play a vital role in oxidative defense systems such as ascorbate, glutathione, tocopherol, flavonoids, alkaloids, and carotenoids [7,8,9]

  • This is because the amino acids, peptides and proteins derived from the food system could function as antioxidants to protect cells and organisms from oxidative damage

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Summary

Introduction

The endogenous enzymes of superoxide dismutase (SOD), catalase, peroxidases, and thioredoxin are responsible for scavenging free radicals and natural antioxidants and play a vital role in oxidative defense systems such as ascorbate, glutathione, tocopherol, flavonoids, alkaloids, and carotenoids [7,8,9]. Once the redox balance is disrupted causing health risks, it is necessary to reinforce the intake of antioxidant groups from food sources. This is because the amino acids, peptides and proteins derived from the food system could function as antioxidants to protect cells and organisms from oxidative damage.

Preparation of Antioxidant Fractions
Solvent Extraction
Enzymatic Hydrolysis
Approaches for Measuring Antioxidant Capacity
Chemical Reactions
Cell Model
Animal Model
Purification and Identification of Antioxidant Peptides
Characteristics of Antioxidant Peptides
Molecular Weight
Constitution and Sequence of Amino Acid
Findings
Implication
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