2018
DOI: 10.1016/j.jff.2018.06.014
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Preparation, identification, and activity evaluation of ten antioxidant peptides from protein hydrolysate of swim bladders of miiuy croaker (Miichthys miiuy)

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Cited by 98 publications
(142 citation statements)
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References 42 publications
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“…The EC 50 value of HFP was 4.90 mg/ml, which was lower than those of HFO from flaxseed (Udenigwe & Aluko, ), and anti‐oxidative oligopeptides from protein hydrolysates of weatherfish loach (PSYV: 17.0 mg/ml) (You, Zhao, Regenstein, & Ren, ) or blue mussel (FLNEFLHV: 4.95 mg/ml) (Ahn, Kim, & Je, ). However, the EC 50 of HFP was higher than those of antioxidant peptides from protein hydrolysates of grass carp skin (VGGRP: 2.94 mg/ml; GFGPL: 2.25 mg/ml) (Cai et al, ), spotless smoothhound cartilage (GAERP: 3.73 mg/ml; GEREANVM: 1.87 mg/ml; AEVG: 2.30 mg/ml) (Tao, Zhao, Chi, & Wang, ), salmon pectoral fin (TTANIEDRR: 2.50 mg/ml) (Ahn, Cho, & Je, ), and swim bladders of miiuy croaker (FPYLRH: 0.51 mg/ml; GIEWA: 0.78 mg/ml) (Zhao et al, ). HFP could donate electrons or hydrogen radicals for inhibiting the DPPH radical reaction.…”
Section: Resultsmentioning
confidence: 99%
“…The EC 50 value of HFP was 4.90 mg/ml, which was lower than those of HFO from flaxseed (Udenigwe & Aluko, ), and anti‐oxidative oligopeptides from protein hydrolysates of weatherfish loach (PSYV: 17.0 mg/ml) (You, Zhao, Regenstein, & Ren, ) or blue mussel (FLNEFLHV: 4.95 mg/ml) (Ahn, Kim, & Je, ). However, the EC 50 of HFP was higher than those of antioxidant peptides from protein hydrolysates of grass carp skin (VGGRP: 2.94 mg/ml; GFGPL: 2.25 mg/ml) (Cai et al, ), spotless smoothhound cartilage (GAERP: 3.73 mg/ml; GEREANVM: 1.87 mg/ml; AEVG: 2.30 mg/ml) (Tao, Zhao, Chi, & Wang, ), salmon pectoral fin (TTANIEDRR: 2.50 mg/ml) (Ahn, Cho, & Je, ), and swim bladders of miiuy croaker (FPYLRH: 0.51 mg/ml; GIEWA: 0.78 mg/ml) (Zhao et al, ). HFP could donate electrons or hydrogen radicals for inhibiting the DPPH radical reaction.…”
Section: Resultsmentioning
confidence: 99%
“…Figure 3B indicated that DPPH• and HO• scavenging activities of MUA-4-B were 86.39% ± 4.32% and 80.56% ± 3.55% at the concentration of 5.0 mg protein/mL, which were significantly higher than those of MUA-4 (DPPH• 76.64% ± 3.43%; HO• 69.39% ± 3.58%) and MUA-4-A (DPPH• 56.38% ± 3.62%; HO• 55.26% ± 4.39%) (p < 0.05). Gel filtration chromatography is a frequently-used prepared technique according to the MW of the separated substances and is applied to separate peptides from protein hydrolysates and their fractions, such as Spanish mackerel [30], miiuy croaker [10,20], ark shell [19], and blue-spotted stingray [22]. Therefore, fraction MUA-4-B was selected for the following isolation process.…”
Section: Gel Filtration Chromatography Of Mua-4mentioning
confidence: 99%
“…The EC 50 values of MMP-4, MMP-7, and MMP-12 were 0.39, 0.62, and 0.51 mg/mL, respectively, but their activities were still lower than that of the positive control of GSH at the same concentration. The EC 50 value of MMP-4 was lower than those of most APs from protein hydrolysates of red stingray cartilages (VPR: 4.61 mg/mL, IEPH: 1.90 mg/mL, LEEEE: 3.69 mg/mL, and IEEEQ: 4.01 mg/mL) [6], loach (PSYV: 17.0 mg/mL) [35], salmon pectoral fin (TTANIEDRR: 2.50 mg/mL) [36], Spanish mackerel skins (PFGPD: 0.80 mg/mL, PYGAKG: 3.02 mg/mL, and YGPM: 0.72 mg/mL) [37], skipjack tuna bone (GADIVA: 0.57 mg/mL) [23], and miiuy croaker swim bladders (FPYLRH: 0.51 mg/mL; GIEWA: 0.78 mg/mL; YLPYA: 3.63 mg/mL; VPDDD: 2.87 mg/mL) [20]. Therefore, the present result suggested that three isolated peptides (MMP-4, MMP-7, and MMP-12), especially MMP-4 could contribute an electron or hydrogen radical to suppress the DPPH• reaction.…”
Section: Dpph Scavenging Activitymentioning
confidence: 99%
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“…Nowadays, a variety of antioxidant peptides have been identified from meat muscles, animals, vegetables, fruits, plant protein, and other foods (Gao et al, 2019;Wu et al, 2018;Yuan et al, 2018;Zhang & Mu, 2017;Zhang, Gao, et al, 2018;Zhao, Luo, et al, 2018;Zhu, Zhang, Zhou, & Xu, 2016). Peptide GWWW isolated from myoglobin showed a strong antioxidant activity against peroxyl radicals, and they suggested that amino acid side chains can be a base to design peptides with activities against some special target ROS and RNS (Karadag, Ozcelik, & Saner, 2009).…”
mentioning
confidence: 99%