Chia Nan University of Pharmacy & Science Institutional Repository:Item 310902800/34431
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    Title: Food-Derived Bioactive Peptides with Antioxidative Capacity, Xanthine Oxidase and Tyrosinase Inhibitory Activity
    Authors: Thaha, Anthony
    Wang, Bor-Sen
    Chang, Yu-Wei
    Hsia, Shih-Min
    Huang, Tsui-Chin
    Shiau, Chyuan-Yuan
    Hwang, Deng-Fwu
    Chen, Tai-Yuan
    Contributors: Natl Taiwan Ocean Univ, Ctr Excellence Oceans, Dep Ftood Sci
    Chia Nan Univ Pharm & Sci, Dept Appl Life Sci & Hlth
    Natl Taiwan Ocean Univ, Inst Food Safety & Risk Management
    Taipei Med Univ, Coll Nutr, Sch Nutr & Hlth Sci
    Taipei Med Univ, Coll Med Sci & Technol, Grad Inst Canc Biol & Drug Discovery
    Keywords: bioactive peptides
    antioxidant
    xanthine oxidase
    tyrosinase
    anti-browning
    enzyme kinetics
    Date: 2021
    Issue Date: 2023-11-11 11:52:25 (UTC+8)
    Publisher: MDPI
    Abstract: Bioactive peptides (BPs) released by proteases from different food protein sources are often served as antioxidants in food applications. This study aims to investigate 11 BPs derived from fish and egg white as potential natural antioxidants by antioxidant activity assays. The kinetic activity of the BPs against xanthine oxidase (XOD) and tyrosinase was also analyzed. The antioxidative capacity of the BPs indicated that VWWW (VW4, mackerel meat), followed by IRW (IW3, egg white) and VKAGFAWTANQQLS (VS14, tuna backbone protein), possessed the highest antioxidant activity in 1,1-diphenyl-2-picrylhydrazyl radical (DPPH), 2,2 '-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) and reducing power (RP) assays. Both the free-radical scavenging score predicted from the AnOxPePred algorithm and the DPPH, ABTS and RP results indicated that VW4 was the best antioxidant. Furthermore, the XOD and tyrosinase inhibition by three selected peptides exhibited competitive patterns of effective inhibition. The half maximal inhibitory concentrations (IC50) of the peptides for XOD inhibition were 5.310, 3.935, and 1.804 mM for VW4, IW3, and VS14, respectively, and they could serve as competitive natural XOD inhibitors. The IC50 of the peptides for tyrosinase inhibition were 1.254, 2.895, and 0.595 mM for VW4, IW3, and VS14, respectively. Overall, VW4, IW3, and VS14 are potential antioxidants and natural XOD inhibitors for preventing milk-fat oxidation, and anti-browning sources for inhibiting food-derived tyrosinase oxidation.
    Relation: PROCESSES, v.9, n.5
    Appears in Collections:[Dept. of Life and Health Science] Periodical Articles

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