Purification of novel antioxidant peptides from myofibrillar protein hydrolysate of chicken breast and their antioxidant potential in chemical and H2O2-stressed cell systems

2021 ◽  
Author(s):  
Jinyu Chen ◽  
Yijun Yan ◽  
Leilei Zhang ◽  
Jiayu Zheng ◽  
Jinting Guo ◽  
...  
Keyword(s):  
Bioactive Peptides ◽  
Protein Hydrolysate ◽  
Myofibrillar Protein ◽  
Chicken Breast ◽  
Muscle Proteins ◽  
Antioxidant Peptides ◽  
Cell Systems ◽  
Stressed Cell ◽  
Promising Source ◽  
Total Muscle

Myofibrillar protein accounting for about 60% of total muscle proteins is expected to be a promising source of bioactive peptides. The purpose of the present study was to purify antioxidant...

Functional peptides from yellowfin tuna (Thunnus albacares): Characterisation and storage stability assessment

2020 ◽  
Vol 67 (2) ◽  
Author(s):  
U. Parvathy ◽  
P. K. Binsi ◽  
S. Visnuvinayagam ◽  
A. A. Zynudheen ◽  
George Ninan ◽  
...  
Keyword(s):  
Bioactive Peptides ◽  
Storage Stability ◽  
Activity Index ◽  
Protein Hydrolysate ◽  
Red Meat ◽  
Yellowfin Tuna ◽  
Raw Material ◽  
Foaming Properties ◽  
Peptide Pattern ◽  
Promising Source

Present study attempted the effective utilisation of tuna red meat which is a major cannery waste from tuna industry, by recovery in the form of bioactive peptides. Protein hydrolysate from yellowfin tuna red meat was, characterised for functional properties. Molecular weight profile of the derived hydrolysate revealed its heterogeneity in peptide pattern with a major distribution above 10 kDa (60%). A protein recovery of 39.64% was obtained from the raw material with a protein content of 88.57±0.66% in the derived tuna protein hydrolysate (TPH). Present study revealed TPH to have rich levels of amino acids like glutamic acid, aspartic acid, lysine and leucine while phenyl alanine, tyrosine, methionine and cysteine were found in lower amounts. Variations in foaming properties at different pH levels ranging from 2-10 indicated these properties to be maximum at pH 6.0. Similarly, emulsion stability index was highest (48.09±2.69 min) at pH of 6.0. However, emulsifying activity index increased with increase in pH. The storage stability studies carried out for TPH at ambient (28oC) and chilled storage conditions (4oC) for upto six months indicated an uptake of moisture, increase in oxidative indices as well as changes in functionality which was more prominent under ambient conditions. Results suggested protein hydrolysate from tuna red meat to be a promising source of bioactive peptides, finding suitability in formulation of functional foods as well as nutraceutical products.

scholarly journals Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

2021 ◽  
Vol 22 (17) ◽  
pp. 9508
Author(s):  
Nhung Thi Phuong Nong ◽  
Jue-Liang Hsu
Keyword(s):  
Bioactive Peptides ◽  
Protein Hydrolysate ◽  
Tyrosine Phosphatase ◽  
Food Protein ◽  
Dpp Iv ◽  
Glucosidase Inhibitors ◽  
Commercial Applications ◽  
Ptp 1B

Diabetes, a glucose metabolic disorder, is considered one of the biggest challenges associated with a complex complication of health crises in the modern lifestyle. Inhibition or reduction of the dipeptidyl peptidase IV (DPP-IV), alpha-glucosidase, and protein-tyrosine phosphatase 1B (PTP-1B) enzyme activities or expressions are notably considered as the promising therapeutic strategies for the management of type 2 diabetes (T2D). Various food protein-derived antidiabetic bioactive peptides have been isolated and verified. This review provides an overview of the DPP-IV, PTP-1B, and α-glucosidase inhibitors, and updates on the methods for the discovery of DPP-IV inhibitory peptides released from food-protein hydrolysate. The finding of novel bioactive peptides involves studies about the strategy of separation fractionation, the identification of peptide sequences, and the evaluation of peptide characteristics in vitro, in silico, in situ, and in vivo. The potential of bioactive peptides suggests useful applications in the prevention and management of diabetes. Furthermore, evidence of clinical studies is necessary for the validation of these peptides’ efficiencies before commercial applications.

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.

Characterization of Muscle Sarcoplasmic and Myofibrillar Protein Hydrolysis Caused by Lactobacillus plantarum

1999 ◽  
Vol 65 (8) ◽  
pp. 3540-3546 ◽  
Author(s):  
Silvina Fadda ◽  
Yolanda Sanz ◽  
Graciela Vignolo ◽  
M.-Concepción Aristoy ◽  
Guillermo Oliver ◽  
...  
Keyword(s):  
Lactobacillus Plantarum ◽  
Myofibrillar Protein ◽  
Myofibrillar Proteins ◽  
Muscle Proteins ◽  
Whole Cells ◽  
Sarcoplasmic Proteins ◽  
Cell Extracts ◽  
Hydrophobic Nature ◽  
Hydrolysis Of

ABSTRACT Strains of Lactobacillus plantarum originally isolated from sausages were screened for proteinase and aminopeptidase activities toward synthetic substrates; on the basis of that screening,L. plantarum CRL 681 was selected for further assays on muscle proteins. The activities of whole cells, cell extracts (CE), and a combination of both on sarcoplasmic and myofibrillar protein extracts were determined by protein, peptide, and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins. The addition of CE intensified the proteolysis. Whole cells generated hydrophilic peptides from both sarcoplasmic and myofibrillar proteins. Other peptides of a hydrophobic nature resulted from the combination of whole cells and CE. The action of both enzymatic sources on myofibrillar proteins caused maximal increases in lysine, arginine, and leucine, while the action of those on sarcoplasmic proteins mainly released alanine. In general, pronounced hydrolysis of muscle proteins required enzyme activities from whole cells in addition to those supplied by CE.

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.

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