A novel bioactive peptide derived from enzymatic hydrolysis of Ruditapes philippinarum: Purification and investigation of its free-radical quenching potential

Kim, Min Jung; Hwang, Jin-Woo; Kim, Yon-Suk; Ahn, Chang‐Bum; Jeon, You‐Jin; Kweon, Hyuk-Jung; Bahk, Young Yil; Moon, Sang-Ho; Jeon, Byong-Tae; Park, Pyo-Jam

doi:10.1016/j.procbio.2012.10.016

Cited by 27 publications

(27 citation statements)

References 35 publications

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“…Peptides having smaller molecular masses are generally believed to have greater antioxidant activity than those having larger masses [25,26]. In accordance with this, during the fractionation of marine invertebrate protein hydrolysates with UF membranes, peptidic fractions having the lowest molecular mass range showed the highest DPPH radical scavenging activity [31,33,36] and the highest hydroxyl radical scavenging activity [42,53]. Similarly, UF fractions with the lowest molecular mass range (<3 kDa), which were prepared from the giant squid muscle [43] and jumbo squid skin gelatin [41], had the highest inhibitory activity against linoleic acid oxidation relative to other UF fractions in the same study.…”

Section: Molecular Characteristics and Structure–activity Relationmentioning

confidence: 90%

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

et al. 2017

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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.

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Section: Molecular Characteristics and Structure–activity Relationmentioning

confidence: 90%

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

et al. 2017

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“…The peptide, Val-Glu-Cys-Tyr-Gly-Pro-Asn-Arg-Pro-Gln-Phe, reported by Sheih et al, was released from pepsin hydrolysate of a microalgae (C. vulgaris), showing the strongest ABTS scavenging activity (IC 50 =9.8±0.5 μM) compared with Trolox, ascorbic acid, and BHT (IC 50 =32.5±1.3, 30.0±0.8 and 57.4±2.3 μM, respectively) [28]. The peptide (Leu-Asn-Gly-Asp-Val-Trp) isolated by Ko et al not only possessed antioxidant activity in DPPH, hydroxyl radical, and ·, alkyl radical [67] peroxyl radical tests (IC 50 =0.92±0.12, 1.42±0.08 and 0.02±0.01 mg/ml), but also protected Vero (Monkey kidney cell line) cells against AAPH-induced damage effectively.…”

Section: Marine Sources Of Antioxidant Peptidesmentioning

confidence: 93%

“…But the antioxidants dissolved in acetonitrile barely show hydroxyl radicals scavenging activity [41]. In vitro, hydroxyl radical can be generated by the ironcatalyzed Fenton reaction [67]. Hydroxyl radicals can oxidize Fe 2+ to Fe 3+ , and only Fe 2+ can combine with 1,10-phenanthroline to form a red compound (1,10-phenanthroline-Fe 2+ ).…”

Section: Hydroxyl Radical Scavenging Assaymentioning

confidence: 99%

Overview of Antioxidant Peptides Derived from Marine Resources: The Sources, Characteristic, Purification, and Evaluation Methods

Wü

Liú

et al. 2015

Appl Biochem Biotechnol

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Marine organisms are rich sources of structurally diverse bioactive nitrogenous components. In recent years, numerous bioactive peptides have been identified in a range of marine protein resources, such as antioxidant peptides. Many studies have approved that marine antioxidant peptides have a positive effect on human health and the food industry. Antioxidant activity of peptides can be attributed to free radicals scavenging, inhibition of lipid peroxidation, and metal ion chelating. Moreover, it has also been verified that peptide structure and its amino acid sequence can mainly affect its antioxidant properties. The aim of this review is to summarize kinds of antioxidant peptides from various marine resources. Additionally, the relationship between structure and antioxidant activities of peptides is discussed in this paper. Finally, current technologies used in the preparation, purification, and evaluation of marine-derived antioxidant peptides are also reviewed.

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“…Trypsin exclusively cleaves Arg or Lys residues on the C terminal, and α-chymotrypsin preferentially cleaves peptide amide bonds and prefers hydrophobic residues, such as Tyr, Trp, or Phe (Kim et al, 2013;Asante et al, 2014). These AA are sensitive to free radicals and transformed into carbonyl groups (Kim et al, 2013).…”

Section: In Vitro Digestibility Of Oxidized Wpimentioning

confidence: 99%

“…The initial slope, maximal rate of digestion, and maximal degradation with trypsin or α-chymotrypsin were higher compared with pepsin. This could be explained by the sensitivity of hydrophobic residues to dual-enzyme system containing α-chymotrypsin (Kim et al, 2013).…”

Section: In Vitro Digestibility Of Oxidized Wpimentioning

confidence: 99%

Susceptibility of whey protein isolate to oxidation and changes in physicochemical, structural, and digestibility characteristics

Feng

Ullah

et al. 2015

Journal of Dairy Science

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Oxidation is an important factor for denaturing of whey protein isolate (WPI) during food processing. We studied the effects of chemical oxidation on physicochemical and structural changes along with in vitro digestibility of WPI in this work. Evaluation of physicochemical changes showed that carbonyl level and dityrosine content increased, whereas total and free thiol group levels decreased for oxidized WPI samples. For the structural changes, protein aggregation was measured by surface hydrophobicity, turbidity, and particle diameter, which was increased for oxidized WPI samples. The increase of the secondary structure β-sheets and antiparallel β-sheet also supported the aggregation of oxidized WPI. A direct quantitative relationship between physicochemical and structural changes and protein digestibility indicated that oxidation-related damage restricts the susceptibility of WPI to proteases. In conclusion, WPI had high susceptibility to oxidative stress, and both physicochemical and structural changes caused by severe oxidative stress could decrease the rate of in vitro digestibility of WPI.

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A novel bioactive peptide derived from enzymatic hydrolysis of Ruditapes philippinarum: Purification and investigation of its free-radical quenching potential

Cited by 27 publications

References 35 publications

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

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

Overview of Antioxidant Peptides Derived from Marine Resources: The Sources, Characteristic, Purification, and Evaluation Methods

Susceptibility of whey protein isolate to oxidation and changes in physicochemical, structural, and digestibility characteristics

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