Enzyme-Assisted Discovery of Antioxidant Peptides from Edible Marine Invertebrates: A Review

Abstract

Marine invertebrates, such as oysters, mussels, clams, scallop, jellyfishes, squids, prawns, sea cucumbers and sea squirts, are consumed as foods. These edible marine invertebrates are sources of potent bioactive peptides. The last two decades have seen a surge of interest in the discovery of antioxidant peptides from edible marine invertebrates. Enzymatic hydrolysis is an efficient strategy commonly used for releasing antioxidant peptides from food proteins. A growing number of antioxidant peptide sequences have been identified from the enzymatic hydrolysates of edible marine invertebrates. Antioxidant peptides have potential applications in food, pharmaceuticals and cosmetics. In this review, we first give a brief overview of the current state of progress of antioxidant peptide research, with special attention to marine antioxidant peptides. We then focus on 22 investigations which identified 32 antioxidant peptides from enzymatic hydrolysates of edible marine invertebrates. Strategies adopted by various research groups in the purification and identification of the antioxidant peptides will be summarized. Structural characteristic of the peptide sequences in relation to their antioxidant activities will be reviewed. Potential applications of the peptide sequences and future research prospects will also be discussed.

Trypsin‐hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects

“…A similar time-dependent increase in lipid peroxidation in the same model was also reported by Karnjanapratum and Benjakul [28] when investigating the antioxidant effect of gelatin hydrolysates derived from unicorn leatherjacket skin. The antioxidant activity of food protein hydrolysates and peptides, particularly in protecting against lipid peroxidation, has been associated with the presence of hydrophobic residues, such as alanine, leucine, and proline [6]. Hence the ability of T1H to repress lipid peroxidation implies the presence of hydrophobic residue-containing peptides in the hydrolysate.…”

Insight into antioxidant properties of milk‐derived bioactive peptides in vitro and in a cellular model

“…Several characteristics, described to explain the antioxidant action of peptides, are based on the properties of the single amino acids such as acid/basic character, hydrophobicity, aromaticity, and hydrogen donating capacity . In addition, also the molecular mass of the amino acids and their sequence in the peptide are relevant in this respect.…”

Housefly Pupae-Derived Antioxidant Peptides Exerting Neuroprotective Effects on Hydrogen Peroxide-Induced Oxidative Damage in PC12 Cells

“…In the last two decades, there has been a marked increase in searching for antioxidant peptides from food products, animals or plants resources [11] due to their higher safety and activity compared to synthetic antioxidants, such as butylated hydroxyanisole (BHA) and butylated hydroxytoluene (BHT) which are reported to have latent acute toxicity, developmental [12] and reproductive toxicity [13].…”