Abstract
In the work, water-soluble proteins of red stingray (Dasyatis akajei) cartilages were extracted by guanidine hydrochloride and hydrolyzed using trypsin. Subsequently, four antioxidant peptides (RSHP-A, RSHP-B, RSHP-C, and RSHP-D) were isolated from the water-soluble protein hydrolysate while using ultrafiltration and chromatographic techniques, and the amino acid sequences of RSHP-A, RSHP-B, RSHP-C, and RSHP-D were identified as Val-Pro-Arg (VPR), Ile-Glu-Pro-His (IEPH), Leu-Glu-Glu--Glu-Glu (LEEEE), and Ile-Glu-Glu-Glu-Gln (IEEEQ), with molecular weights of 370.46 Da, 494.55 Da, 647.64 Da, and 646.66 Da, respectively. VPR, IEPH, LEEEE, and IEEEQ exhibited good scavenging activities on the DPPH radical (EC50 values of 4.61, 1.90, 3.69, and 4.01 mg/mL, respectively), hydroxyl radical (EC50 values of 0.77, 0.46, 0.70, and 1.30 mg/mL, respectively), superoxide anion radical (EC50 values of 0.08, 0.17, 0.15, and 0.16 mg/mL, respectively), and ABTS cation radical (EC50 values of 0.15, 0.11, 0.19, and 0.18 mg/mL, respectively). Among the four isolated antioxidant peptides, IEPH showed the strongest reducing power and lipid peroxidation inhibition activity, but LEEEE showed the highest Fe2+-chelating ability. The present results suggested that VPR, IEPH, LEEEE, and IEEEQ might have the possibility of being an antioxidant additive that is used in functional food and pharmaceuticals.
Highlights
Superfluous reactive oxygen species (ROS) are produced under oxidative stress conditions and they can destroy all types of macromolecules, which further lead to many health disorders, such as cancer, diabetes mellitus, and inflammatory diseases [1,2,3]
Bioactive peptides are inactive in the sequence of their parent proteins and they can be released by enzymatic hydrolysis either during gastrointestinal digestion in the body or during food processing [2]
Bioactive peptides may actcompounds as regulatory compounds with diverse biological liberated from protein sources by proteolysis, such as antioxidant, antihypertensive, and enhancing once they are liberated from protein sources by proteolysis, such as antioxidant, antihypertensive, immunity activities
Summary
Superfluous reactive oxygen species (ROS) are produced under oxidative stress conditions and they can destroy all types of macromolecules, which further lead to many health disorders, such as cancer, diabetes mellitus, and inflammatory diseases [1,2,3]. Antioxidant peptides (APs) from food resources usually contain 2–20 amino acid residues and they can donate hydrogen, trap lipid-derived free radicals, and/or activate antioxidant enzymes in cells [5,6,7,8,9,10]. APs can convert ROS, including superoxide anion radicals 2 ) and hydroxyl radicals (HO) into stable molecular structure to inhibit the propagation of peroxidizing chain reaction [5,6,7,8,9,10]. FWKVV and FMPLH were isolated from the protein hydrolysate of miiuy croaker (Miichthys miiuy) muscle and exhibited strong reducing power, lipid peroxidation inhibition ability, and radical scavenging activity [9]. The AP fractions of CPF1 (molecular weight (MW) < 1 kDa) and CPF2
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