Preparation, identification, and activity evaluation of ten antioxidant peptides from protein hydrolysate of swim bladders of miiuy croaker (Miichthys miiuy)

2018 ◽  
Vol 47 ◽  
pp. 503-511 ◽  
Author(s):  
Wen-Hao Zhao ◽  
Qian-Bin Luo ◽  
Xin Pan ◽  
Chang-Feng Chi ◽  
Kun-Lai Sun ◽  
...  
Keyword(s):  
Protein Hydrolysate ◽  
Antioxidant Peptides ◽  
Activity Evaluation ◽  
Miichthys Miiuy

scholarly journals Antioxidant Peptides from the Protein Hydrolysate of Spanish Mackerel (Scomberomorous niphonius) Muscle by in Vitro Gastrointestinal Digestion and Their in Vitro Activities

Marine Drugs ◽  
2019 ◽  
Vol 17 (9) ◽  
pp. 531 ◽  
Author(s):  
Zhao ◽  
Yang ◽  
Wang ◽  
Zhao ◽  
Chi ◽  
...  
Keyword(s):  
Protein Hydrolysate ◽  
Radical Scavenging ◽  
Model Systems ◽  
Dpph Radical ◽  
Antioxidant Peptides ◽  
Gastrointestinal Digestion ◽  
Spanish Mackerel ◽  
In Vitro Gastrointestinal Digestion ◽  
Dpph Radical Scavenging

For the full use of Spanish mackerel (Scomberomorous niphonius) muscle to produce antioxidant peptides, the proteins of Spanish mackerel muscle were separately hydrolyzed under five kinds of enzymes and in vitro gastrointestinal digestion, and antioxidant peptides were isolated from the protein hydrolysate using ultrafiltration and multiple chromatography methods. The results showed that the hydrolysate (SMPH) prepared using in vitro GI digestion showed the highest degree of hydrolysis (27.45 ± 1.76%) and DPPH radical scavenging activity (52.58 ± 2.68%) at the concentration of 10 mg protein/mL among the six protein hydrolysates, and 12 peptides (SMP-1 to SMP-12) were prepared from SMPH. Among them, SMP-3, SMP-7, SMP-10, and SMP-11 showed the higher DPPH radical scavenging activities and were identified as Pro-Glu-Leu-Asp-Trp (PELDW), Trp-Pro-Asp-His-Trp (WPDHW), and Phe-Gly-Tyr-Asp-Trp-Trp (FGYDWW), and Tyr-Leu-His-Phe-Trp (YLHFW), respectively. PELDW, WPDHW, FGYDWW, and YLHFW showed high scavenging activities on DPPH radical (EC50 1.53, 0.70, 0.53, and 0.97 mg/mL, respectively), hydroxyl radical (EC50 1.12, 0.38, 0.26, and 0.67 mg/mL, respectively), and superoxide anion radical (EC50 0.85, 0.49, 0.34, and 1.37 mg/mL, respectively). Moreover, PELDW, WPDHW, FGYDWW, and YLHFW could dose-dependently inhibit lipid peroxidation in the linoleic acid model system and protect plasmid DNA (pBR322DNA) against oxidative damage induced by H2O2 in the tested model systems. In addition, PELDW, WPDHW, FGYDWW, and YLHFW could retain their high activities when they were treated under a low temperature (<60 °C) and a moderate pH environment (pH 5–9). These present results indicate that the protein hydrolysate, fractions, and isolated peptides from Spanish mackerel muscle have strong antioxidant activity and might have the potential to be used in health food products.

scholarly journals Four Antioxidant Peptides from Protein Hydrolysate of Red Stingray (Dasyatis akajei) Cartilages: Isolation, Identification, and In Vitro Activity Evaluation

Marine Drugs ◽  
2019 ◽  
Vol 17 (5) ◽  
pp. 263 ◽  
Author(s):  
Xiao-Yang Pan ◽  
Yu-Mei Wang ◽  
Li Li ◽  
Chang-Feng Chi ◽  
Bin Wang
Keyword(s):  
Protein Hydrolysate ◽  
Guanidine Hydrochloride ◽  
Cation Radical ◽  
Reducing Power ◽  
Amino Acid Sequences ◽  
Water Soluble ◽  
Antioxidant Peptides ◽  
Antioxidant Additive ◽  
Dasyatis Akajei ◽  
Red Stingray

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.

scholarly journals Prediction and Identification of Antioxidant Peptides in Potato Protein Hydrolysate

2020 ◽  
Vol 2020 ◽  
pp. 1-10
Author(s):  
Juan Wu ◽  
Chao Mao ◽  
Wenli Zhang ◽  
Yu Cheng
Keyword(s):  
Amino Acid ◽  
Protein Hydrolysate ◽  
Gel Filtration ◽  
Principal Component ◽  
Antioxidant Peptides ◽  
Potato Protein ◽  
Amino Acid Compositions ◽  
Rp Hplc ◽  
Scavenging Capacity ◽  
Component Matrix

Principal component analysis (PCA) was used to cluster the possible amino acid compositions of antioxidant peptides in potato protein hydrolysate (PPH). The antioxidant peptides exhibiting high ABTS+• scavenging capacity were isolated with the procedure of ultrafiltration, gel filtration, and preparative RP-HPLC and identified by UPLC-MS/MS. Phe, Tyr, and His were shown to group together with ABTS+• scavenging capacity in component matrix plot. Three prominent peptides, namely, Phe-Tyr, Tyr-Phe-Glu, and Pro-Pro-His-Tyr-Phe, which matched the sequence of patatin and were made up of Phe and Tyr, were identified. The peptide Tyr-Phe-Glu demonstrated antioxidant activity against Caco-2 cell oxidation induced by H2O2. The results suggested that multivariate analysis could be used to predict the amino acid compositions of antioxidant peptides.

scholarly journals Preparation, Identification, and Activity Evaluation of Eight Antioxidant Peptides from Protein Hydrolysate of Hairtail (Trichiurus japonicas) Muscle

Marine Drugs ◽  
2019 ◽  
Vol 17 (1) ◽  
pp. 23 ◽  
Author(s):  
Xiu-Rong Yang ◽  
Lun Zhang ◽  
Dong-Ge Ding ◽  
Chang-Feng Chi ◽  
Bin Wang ◽  
...  
Keyword(s):  
Superoxide Anion ◽  
Protein Hydrolysate ◽  
Reducing Power ◽  
Model System ◽  
Amino Acid Sequences ◽  
Health Food ◽  
Antioxidant Peptides ◽  
Food Industries ◽  
Molecular Weights ◽  
Hydrolysis Process

In this report, protein of hairtail (Trichiurus japonicas) muscle was separately hydrolyzed using five kinds of proteases (alcalase, trypsin, neutrase, pepsin, and papain), and the papain- and alcalase-hydrolysates showed higher 2,2-diphenyl-1-picrylhydrazyl radicals (DPPH•) and hydroxyl radical (HO•) scavenging activity than other three protease hydrolysates. Therefore, the protein hydrolysate of hairtail muscle (HTP) was prepared using binary-enzymes hydrolysis process (papain + alcalase). Subsequently, eight antioxidant peptides were purified from HTP using membrane ultrafiltration and chromatography technology, and their amino acid sequences were identified as Gln-Asn-Asp-Glu-Arg (TJP1), Lys-Ser (TJP2), Lys-Ala (TJP3), Ala-Lys-Gly (TJP4), Thr-Lys-Ala (TJP5), Val-Lys (TJP6), Met-Lys (TJP7), and Ile-Tyr-Gly (TJP8) with molecular weights of 660.3, 233.0, 217.1, 274.1, 318.0, 245.1, 277.0, and 351.0 Da, respectively. TJP3, TJP4, and TJP8 exhibited strong scavenging activities on DPPH• (EC50 0.902, 0.626, and 0.663 mg/mL, respectively), HO• (EC50 1.740, 2.378, and 2.498 mg/mL, respectively), superoxide anion radical (EC50 2.082, 2.538, and 1.355 mg/mL, respectively), and 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical (EC50 1.652, 0.831, and 0.586 mg/mL, respectively). Moreover, TJP3, TJP4, and TJP8 showed higher reducing power and inhibiting ability on lipid peroxidation in a linoleic acid model system. These results suggested that eight isolated peptides (TJP1 to TJP8), especially TJP3, TJP4, and TJP8 might serve as potential antioxidants applied in the pharmaceutical and health food industries.

Potential Use of Tuna (Thunnus albacares) by-product: Production of Antioxidant Peptides and Recovery of Unsaturated Fatty Acids from Tuna Head

2017 ◽  
Vol 13 (7) ◽  
Author(s):  
Dayse Oliveira ◽  
Daniela Bernardi ◽  
Fernanda Drummond ◽  
Fabiana Dieterich ◽  
Wilson Boscolo ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Antioxidant Capacity ◽  
Unsaturated Fatty Acids ◽  
Protein Hydrolysate ◽  
Trolox Equivalent Antioxidant Capacity ◽  
Total Amino Acid ◽  
Degree Of Hydrolysis ◽  
Antioxidant Peptides ◽  
Antioxidant Power ◽  
By Products

AbstractTuna by-products were subjected to enzymatic hydrolysis with Alcalase (enzyme to substrate ratio 1 : 200 w/w; 60 °C; pH 6.5, 120 min) rendering a tuna protein hydrolysate (TPH) with 9.24 % degree of hydrolysis (DH). The antioxidant capacity of TPH determined by the methods of ferric reducing antioxidant power (FRAP) and Trolox equivalent antioxidant capacity (TEAC) were similar and 10 times lower than the result obtained by oxygen radical absorbance capacity (ORAC). The total amino acid profile indicated that 42.15 % are composed of hydrophobic amino acids and 7.7 % of aromatics, with leucine being found in the highest quantity (17.85 %). The fatty acid profile of the oil recovered by centrifugation of the TPH – as determined by a gas chromatograph – was characterized by a high percentage of polyunsaturated fatty acids (PUFAs) (39.06 %), mainly represented by the fatty acids ω3, docosahexaenoic acid (27.15 %) and eicosapentaenoic acid (6.05 %). The simultaneous recovery of unsaturated fatty acids and antioxidant peptides can add value to tuna by-products, assisting in the efficient management of fishing industry waste.

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