scholarly journals Gelatin and Antioxidant Peptides from Gelatin Hydrolysate of Skipjack Tuna (Katsuwonus pelamis) Scales: Preparation, Identification and Activity Evaluation

Marine Drugs ◽  
2019 ◽  
Vol 17 (10) ◽  
pp. 565 ◽  
Author(s):  
Qiu ◽  
Wang ◽  
Yang ◽  
Zhao ◽  
Chi ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Amino Acid ◽  
Sodium Dodecyl ◽  
Radical Scavenging ◽  
Ionization Mass ◽  
Type I ◽  
Skipjack Tuna ◽  
Antioxidant Peptides ◽  
Katsuwonus Pelamis ◽  
Gelatin Hydrolysate

For full use of fish by-products, scale gelatin (TG) and antioxidant peptides (APs) of skipjack tuna (Katsuwonus pelamis) were prepared, and their properties were characterized using an amino acid analyzer, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Fourier transform infrared spectroscopy (FTIR), electrospray ionization mass spectrometers (ESI-MS), and radical scavenging assays. The results indicate that TG with a yield of 3.46 ± 0.27% contained Gly (327.9 ± 5.2 residues/1000 residues) as the major amino acid and its imino acid content was 196.1 residues/1000 residues. The structure of TG was more unstable than that of type I collagen from scales of skipjack tuna (TC) and TG was more suitable for preparation of hydrolysate by protease than mammalian gelatins. Therefore, TG was separately hydrolyzed under five proteases (pepsin, papain, trypsin, neutrase, and alcalase) and ten APs (TGP1–TGP10) were isolated from the alcalase-hydrolysate. Among them, TGP5, TGP7, and TGP9 with high antioxidant activity were identified as His-Gly-Pro-Hyp-Gly-Glu (TGP5), Asp-Gly-Pro-Lys-Gly-His (TGP7) and Met-Leu-Gly-Pro-Phe-Gly-Pro-Ser (TGP9), respectively. Furthermore, TGP5, TGP7, and TGP9 exhibited a high radical scavenging capability on 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (EC50 values of 1.34, 0.54, and 0.67 mg/mL, respectively), hydroxyl radical (EC50 values of 1.03, 0.41, and 0.74 mg/mL, respectively), and superoxide anion radical (EC50 values of 1.19, 0.71, and 1.59 mg/mL, respectively). These results suggest that three APs (TGP5, TGP7, and TGP9), especially TGP7, have a strong antioxidant activity and could act as potential antioxidant ingredients applied in functional products.

scholarly journals Preparation and Characterization of Gelatin and Antioxidant Peptides from Gelatin Hydrolysate of Skipjack Tuna (Katsuwonus pelamis) Bone Stimulated by in vitro Gastrointestinal Digestion

Marine Drugs ◽  
2019 ◽  
Vol 17 (2) ◽  
pp. 78 ◽  
Author(s):  
Xiu-Rong Yang ◽  
Yu-Qin Zhao ◽  
Yi-Ting Qiu ◽  
Chang-Feng Chi ◽  
Bin Wang
Keyword(s):  
Amino Acid ◽  
Type I Collagen ◽  
Type I ◽  
Skipjack Tuna ◽  
Antioxidant Peptides ◽  
Gastrointestinal Digestion ◽  
Katsuwonus Pelamis ◽  
In Vitro Gastrointestinal Digestion ◽  
Gelatin Hydrolysate

In China, a large amount of fish bones are produced during the processing of tuna cans production. For full use of those by-products, gelatin (STB-G) with a yield of 6.37 ± 0.64% was extracted from skipjack tuna (Katsuwonus pelamis) bone using water at 60 °C for 8 h. Amino acid analysis showed that STB-G contained Gly (340.3 residues/1000 residues) as the major amino acid and its imino acid content was 177.3 residues/1000 residues. Amino acid composition, SDS-PAGE, and Fourier transform infrared (FTIR) spectrum investigations confirmed that the physicochemical properties of STB-G were similar to those of type I collagen from skipjack tuna bone (STB-C), but partial high molecular weight components of STB-G were degraded during the extraction process, which induced that the gelatin was easier to be hydrolyzed by protease than mammalian gelatins and was suitable for preparation of hydrolysate. Therefore, STB-G was hydrolyzed under in vitro gastrointestinal digestion (pepsin-trypsin system) and five antioxidant peptides were purified from the resulted hydrolysate (STB-GH) and identified as GPDGR, GADIVA, GAPGPQMV, AGPK, and GAEGFIF, respectively. Among the gelatin hydrolysate, fractions, and isolated peptides, GADIVA and GAEGFIF exhibited the strongest scavenging activities on 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (EC50 0.57 and 0.30 mg/mL), hydroxyl radical (EC50 0.25 and 0.32 mg/mL), superoxide anion radical (EC50 0.52 and 0.48 mg/mL), and 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical (EC50 0.41 and 0.21 mg/mL). Moreover, GADIVA and GAEGFIF showed a high inhibiting ability on lipid peroxidation in a linoleic acid model system. The strong activities of five isolated peptides profited by their small molecular sizes and the antioxidant amino acid residues in their sequences. These results suggested that five isolated peptides (STP1–STP5), especially GADIVA and GAEGFIF, might serve as potential antioxidants applied in health food industries.

scholarly journals Identification and Active Evaluation of Antioxidant Peptides from Protein Hydrolysates of Skipjack Tuna (Katsuwonus pelamis) Head

Antioxidants ◽  
2019 ◽  
Vol 8 (8) ◽  
pp. 318 ◽  
Author(s):  
Lun Zhang ◽  
Guo-Xu Zhao ◽  
Yu-Qin Zhao ◽  
Yi-Ting Qiu ◽  
Chang-Feng Chi ◽  
...  
Keyword(s):  
Radical Scavenging ◽  
Reducing Power ◽  
Ionization Mass ◽  
Skipjack Tuna ◽  
Antioxidant Peptides ◽  
Katsuwonus Pelamis ◽  
System Method ◽  
Antioxidant Agents ◽  
Protein Sequencer

For the full use of fish by-products to produce antioxidant peptides, skipjack tuna (Katsuwonus pelamis) heads generated during can processing were defatted and hydrolyzed using the in vitro gastrointestinal (GI) digestion (pepsin–trypsin system) method and six antioxidant peptides (P1 to P6) were purified from the head hydrolysate (KPH) using ultrafiltration and serial chromatography methods. Six isolated peptides (P1 to P6) were identified as Val-Glu-Glu (VEE, P1), Trp-Met-Phe-Asp-Trp (WMFDW, P2), Asp-Ala-Gly-Pro-Tyr-Gly-Pro-Ile (DAGPYGPI, P3), Trp-Met-Gly-Pro-Tyr (WMGPY, P4), Glu-Arg-Gly-Pro-Leu-Gly-Pro-His (ERGPLGPH, P5), and Glu-Met- Gly-Pro-Ala (EMGPA, P6), respectively, using a protein sequencer and electrospray ionization-mass spectrometer. Among skipjack tuna head hydrolysates, fractions, and six isolated peptides (P1 to P6), WMFDW (P2), WMGPY (P4), and EMGPA (P6) showed the highest radical scavenging activities on 2,2-diphenyl-1-picrylhydrazyl (DPPH) (EC50 values of 0.31, 0.33, and 0.46 mg/mL for WMFDW, WMGPY, and EMGPA, respectively), hydroxyl (EC50 values of 0.30, 0.43, and 0.52 mg/mL for WMFDW, WMGPY, and EMGPA, respectively), and superoxide anion (EC50 values of 0.56, 0.38, and 0.71 mg/mL for WMFDW, WMGPY, and EMGPA, respectively). Moreover, WMFDW, WMGPY, and EMGPA showed strong capability in reducing power and lipd peroxidation inhibition in the linoleic acid system. In addition, WMFDW, WMGPY, and EMGPA can retain strong antioxidant activity at temperatures lower than 60 °C and pH values ranged from 5 to 9. The results showed that six isolated peptides (P1 to P6) from skipjack tuna heads, especially WMFDW, WMGPY, and EMGPA, might be applied in health care products acting as powerful antioxidant agents.

scholarly journals Purification and Identification of Antioxidant Peptides from Schizochytrium Limacinum Hydrolysates by Consecutive Chromatography and Electrospray Ionization-Mass Spectrometry

Molecules ◽  
2019 ◽  
Vol 24 (16) ◽  
pp. 3004 ◽  
Author(s):  
Xiao Hu ◽  
Xianqing Yang ◽  
Qiong Wu ◽  
Laihao Li ◽  
Yanyan Wu ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Electrospray Ionization ◽  
High Performance ◽  
Radical Scavenging ◽  
Gel Filtration ◽  
Reducing Power ◽  
Ionization Mass ◽  
Antioxidant Peptides ◽  
Schizochytrium Limacinum ◽  
Radical Scavenging Ability

Schizochytrium limacinum residue was hydrolyzed with various proteases (papain, trypsin, Flavourzyme, Protamex, and Alcalase 2.4L) to obtain antioxidative peptides. The results showed that the S. limacinum hydrolysates (SLHs) prepared with compound proteases (Protamex and Alcalase 2.4L) had the highest antioxidant activity, which was measured using methods such as 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging ability (IC50 = 1.28 mg/mL), hydroxyl radical scavenging ability (IC50 = 1.66 mg/mL), and reducing power (1.42 at 5.0 mg/mL). The hydrolysates were isolated and purified by ultrafiltration, gel filtration chromatography, and reverse-phase high-performance liquid chromatography (RP-HPLC). Through analysis of electrospray ionization-mass spectrometer (ESI-MS/MS), the purified antioxidant peptide was identified as Pro-Tyr-Lys (406 Da). Finally, the identified peptide was synthesized for evaluating its antioxidant activity. The •OH scavenging ability and reducing power of Pro-Tyr-Lys were comparable to those of reduced L-glutathione (GSH). These results demonstrated that the antioxidant peptides from SLHs could potentially be used as effective antioxidants.

scholarly journals Isolation and Identification of Anthocyanin Component in the Fruits of Acanthopanax Sessiliflorus (Rupr. & Maxim.) Seem. by Means of High Speed Counter Current Chromatography and Evaluation of Its Antioxidant Activity

Molecules ◽  
2020 ◽  
Vol 25 (8) ◽  
pp. 1781 ◽  
Author(s):  
Liang Chen ◽  
Xiulan Xin ◽  
Hui Feng ◽  
Shuangshi Li ◽  
Qiguang Cao ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
High Speed ◽  
Radical Scavenging ◽  
Ionization Mass ◽  
Anthocyanin Content ◽  
Separation And Purification ◽  
Isolation And Identification ◽  
Antioxidant Power ◽  
Acanthopanax Sessiliflorus ◽  
Counter Current

Acanthopanax sessiliflorus (Rupr. & Maxim.) Seem. (Araliaceae) is one of the most abundant species of genus Acanthopanax. The fruits of A. sessiliflorus are used in traditional medical protocols as an analgesic, tonic, antidiabetic, antihypertensive, anti-inflammatory, antitumor, and immune-stimulating agent. In this work, we carried out a comprehensive investigation into the anthocyanin components in the fruits of A. sessiliflorus. The anthocyanin content in the fresh fruits of A. sessiliflorus was determined by high performance liquid chromatography-diode array detection (HPLC/DAD), and the anthocyanin component was isolated from these using high-speed counter-current chromatography (HSCCC) and elucidated by electro-spray ionization-mass spectrometry (ESI/MS), 1H- and 13C-NMR. Its antioxidant activity was evaluated by ferric-reducing antioxidant power (FRAP) and 2,2-diphenyl-1-picrylhydrazyl (DPPH). We found that A. sessiliflorus contained a gross anthocyanin content of 121.35 mg/100 g. HSCCC was successfully used for separation and purification of the primary anthocyanin component, cyanidin 3-xylosyl-galactoside. The antioxidant and radical scavenging tests indicated that cyanidin 3-xylosyl-galactoside is a potent antioxidant.

scholarly journals Separation and Enrichment of Antioxidant Peptides from Whey Protein Isolate Hydrolysate by Aqueous Two-Phase Extraction and Aqueous Two-Phase Flotation

Foods ◽  
2019 ◽  
Vol 8 (1) ◽  
pp. 34 ◽  
Author(s):  
Bin Jiang ◽  
Jiaxin Na ◽  
Lele Wang ◽  
Dongmei Li ◽  
Chunhong Liu ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Liquid Chromatography ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Free Radical Scavenging ◽  
Phase Extraction ◽  
Scavenging Activity ◽  
Antioxidant Peptides ◽  
Two Phase ◽  
Aqueous Two Phase Extraction

At present, peptides are separated by molecular exclusion chromatography and liquid chromatography. A separation method is needed in any case, which can be scaled up for industrial scale. In this study, aqueous two-phase extraction (ATPE) and aqueous two-phase flotation (ATPF) were applied to separate and enrich antioxidant peptides from trypsin hydrolysates of whey protein isolates (WPI). The best experimental conditions were investigated, and the results were evaluated using the 2,2′-Azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS) free radical scavenging activity of the peptides-per-unit concentration and the recovery rate (Y) of peptides in the top phase of both ATPE and ATPF. Under optimal conditions, the Y and ABTS free radical scavenging activity per unit concentration in top phase of ATPE could reach 38.75% and 12.94%, respectively, and in ATPF could reach 11.71% and 29.18%, respectively. The purified peptides were characterized by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) and reversed-phase high-performance liquid chromatography (RP-HPLC). PeptideCutter and PeptideMass were applied to analyze and calculate the peptide sequencing. KILDKVGINYWLAHK, VGINYWLAHKALCSEK, and TPEVDDEALEKFDKALK sequences having antioxidant activity were detected in the top phase of ATPE, and VGINYWLAHKALCSEK, KILLDKVGINYWLAHK, ILLDKVGINYWLAHK, IIAEKTKIPAVFK, KIIAEKTKIPAVFK, and VYVEELKPTPEGDLEILLQK sequences having antioxidant activity were detected in the top phase of ATPF. In conclusion, antioxidant peptides were successfully separated from the WPI hydrolysate by ATPE and ATPF; compared with ATPE, ATPF has superior specificity in separating antioxidant peptides.

scholarly journals Mongolian crude propolis content analysis and antioxidant activity

2019 ◽  
Vol 27 (02) ◽  
pp. 34-39
Author(s):  
Ichinkhorloo P ◽  
Gantsetseg G ◽  
Selenge Kh ◽  
Undrakhbayar Ts ◽  
Otgonsugar P ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Amino Acid ◽  
Radical Scavenging ◽  
Antioxidant Effect ◽  
Chemical Components ◽  
Total Amino Acid ◽  
Geographic Origins ◽  
Chemical Content ◽  
High Antioxidant Activity ◽  
Dpph Radical Scavenging

Propolis, a precious bee product has been widely used for pharmaceutical purposes for centuries. Chemical components, properties, and activities are differed based on geographic origins, respective plant sources, and bee species. In our research, Mongolian propolis from 2 different places was examined for chemical content and antioxidant effect. The samples were collected from Northern and Central parts of Mongolia and were examined for a total of 8 contents. Crude Mongolian propolis sample from central part of Mongolia displayed higher results in every aspect with total moisture of 2.1%; ash 1.7%; fat 67.8, 69.3%; and 1.05% of protein. The free amino acid in 70% EtOH was higher in sample from northern part with 1.21µg/mg and the total amino acid was quantified by HPLC and highest concentration detected in methionine 1.90mg/g, and 2.62 mg/g. Totally 3 alkaloids and 2 phenolic were detected by TLC and high antioxidant activity was presented in DPPH radical scavenging test. The results suggest that the best solvent for propolis samples is EtOH 70% solution. The test propolis samples contain different types of alkaloids and phenolic, have high amount of methionine and has high antioxidant effect. 

scholarly journals ANTIOXIDANT ACTIVITY, AMINO ACID PROFILE AND MICROBIAL QUALITY OF BEBONTOT, A BALINESE TRADITIONAL FERMENTED CHICKEN MEAT PRODUCTS

2019 ◽  
Vol 22 (3) ◽  
pp. 93
Author(s):  
Okarini I. A. ◽  
H. Purnomo ◽  
Aulanni'am . ◽  
L. E. Radiati
Keyword(s):  
Antioxidant Activity ◽  
Amino Acid ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Meat Products ◽  
Chicken Meat ◽  
Plate Count ◽  
Total Phenolic ◽  
Microbial Quality

Antioxidant activity, amino acids profile and microbial quality of raw bebontot of chicken meat of spent laying henwere investigated. The samples were prepared using meat dices (1.5 x 2.0 cm) mixed with fresh ground coriander,garlic, galangal, white pepper, salt, sugar and coconut oil then wrapped in Areca catechu palm dried sheaths andfinally fermented spontaneously by drying under the sun for 5 days. The results showed there was a decreasing inpH value, moisture content and 1,1-diphenyl-2-picrylhydrazyl radical scavenging activity of final products, whileits total phenolic content was increasing. Glutamic acid was the most abundant amino acid in products after 5days fementation, followed by tyrosine, aspartic acid, lysine, leucine and histidine. The total plate count and lacticacid bacteria counts were decreasing to 9.39 log cfu/g and 8.98 log cfu/g; the Micrococcaceae was decreased to5.31 log cfu/g; the yeast and moulds counts were increased to 8.58 log cfu/g and 6.51 log cfu/g at the final stageof fermentation. It can be concluded that bebontot chicken meat in this study is a good source of natural phenolicantioxidant, and the present microorganisms will provide the source for the selection of strains well adapted to theenvironment and able to compete with contaminant bacteria.

Purification of human von Willebrand factor–cleaving protease and its identification as a new member of the metalloproteinase family

Blood ◽  
2001 ◽  
Vol 98 (6) ◽  
pp. 1662-1666 ◽  
Author(s):  
Kazuo Fujikawa ◽  
Hiroshi Suzuki ◽  
Brad McMullen ◽  
Dominic Chung
Keyword(s):  
Amino Acid ◽  
Von Willebrand Factor ◽  
Sodium Dodecyl ◽  
Limited Proteolysis ◽  
Single Letter ◽  
Type I ◽  
Commercial Preparation ◽  
Amino Terminal ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract von Willebrand factor (vWF) is synthesized in megakaryocytes and endothelial cells as a very large multimer, but circulates in plasma as a group of multimers ranging from 500 to 10 000 kd. An important mechanism for depolymerization of the large multimers is the limited proteolysis by a vWF-cleaving protease present in plasma. The absence or inactivation of the vWF-cleaving protease results in the accumulation of large multimers, which may cause thrombotic thrombocytopenic purpura. The vWF-cleaving protease was first described as a Ca++-dependent proteinase with an apparent molecular weight of approximately 300 kd. Thus far, however, it has not been isolated and characterized. In this study, the purification of human vWF-cleaving protease from a commercial preparation of factor VIII/vWF concentrate by means of several column chromatographic steps, including 2 steps of heparin-Sepharose column, is reported. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis of the anion exchange and gel filtration column fractions showed that the vWF-cleaving protease activity corresponded to a protein band of 150 kd. After reduction, it migrated with an apparent weight of 190 kd. The amino terminal sequence of the 150-kd band was AAGGIL(H)LE(L)L(D)AXG(P)X(V)XQ (single-letter amino acid codes), with the tentative residues shown in parentheses. A search of the human genome sequence identified the vWF-cleaving protease as a new member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin type I motif) family of metalloproteinase. An active site sequence of HEIGHSFGLEHE (single-letter amino acid codes) was located at 150 residues from the N terminus of the protein.

scholarly journals Polymeric C-terminal cross-linked material from type-I collagen. A modified method for purification, anomalous behaviour on gel filtration, molecular weight estimation, carbohydrate content and lipid content

1980 ◽  
Vol 189 (1) ◽  
pp. 111-124 ◽  
Author(s):  
N D Light ◽  
A J Bailey
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Type I ◽  
Molecular Weight Range ◽  
Carbohydrate Analysis ◽  
Weight Range

Polymeric cross-linked C-terminal peptide material (poly-alpha 1CB6) from mature bovine tendon type-I collagen was prepared and purified by a modification of the method previously described [Light & Bailey (1980) Biochem. J. 185, 373-381]. Poly-alpha 1CB6 was shown to exhibit concentration-dependent aggregation effects on gel filtration due to interaction with a filtration medium. The material had an amino acid content that was very similar to a mixture of alpha 1CB6 and alpha 1CB5. The material was shown to be polydisperse with a mol.wt. range of 50 000-350 000, but chromatographic fractions were relatively homogeneous over this molecular weight range with respect to amino-acid composition. The heterogeneity of the material was not due to incomplete CNBr peptide cleavage, as poly-alpha 1CB6 did not contain detectable quantities of methionine. The material showed no discrete bands on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis but gave a constant blue stain throughout the molecular weight range described above. Lipid analysis showed that the partially purified material contained elevated levels of stearate when compared to the crude CNBr-digested starting material. This may indicate the specific association of a stearic-acid-rich lipid with the peptide material. On carbohydrate analysis poly-alpha 1CB6 was shown to contain only galactose and glucose at levels of 0.72 and 0.28% respectively. The carbohydrate and amino acid analyses indicated that (alpha 1CB6)2-(alpha 1CB5)1 may be the basic cross-linked structural unit of poly-alpha 1CB6)2-(alpha 1CB5)1 units, although the carbohydrate analysis indicated that the higher molecular weight oligomers may be enriched in alpha 1CB6.

scholarly journals Antioxidant and Chelating Activity of NontoxicJatropha curcasL. Protein Hydrolysates Produced byIn VitroDigestion Using Pepsin and Pancreatin

2015 ◽  
Vol 2015 ◽  
pp. 1-9 ◽  
Author(s):  
Santiago Gallegos Tintoré ◽  
Cristina Torres Fuentes ◽  
Javier Solorza Feria ◽  
Manuel Alaiz ◽  
Julio Girón Calle ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Cell Cultures ◽  
Positive Impact ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Protein Hydrolysates ◽  
Ionization Mass ◽  
Chelating Activity ◽  
Metal Chelating ◽  
Functional Components

The antioxidant and metal chelating activities inJ. curcasprotein hydrolysates have been determined. The hydrolysates were produced by treatment of a nontoxic genotype with the digestive enzymes pepsin and pancreatin and then were characterized by fast protein liquid chromatography and reverse phase chromatography. Peptidic fractions with higher radical scavenging activity were analysed by matrix-assisted laser desorption/ionization mass spectrometry. The antioxidant activity was determined by measuring inhibition of the oxidative degradation ofβ-carotene and by measuring the reactive oxygen species (ROS) in Caco-2 cell cultures. Cu2+and Fe2+chelating activities were also determined. The hydrolysates inhibited the degradation ofβ-carotene and the formation of ROS in Caco-2 cells. The lower molecular weight peptidic fractions from FPLC had stronger antioxidant activity in cell cultures compared with the hydrolysates, which correlated with a higher content in antioxidant and chelating amino acids. These fractions were characterized by a large presence of peptides with different molecular masses. The hydrolysates exhibited both Cu2+and Fe2+chelating activity. It was concluded thatJ. curcasis a good source of antioxidant and metal chelating peptides, which may have a positive impact on the economic value of this crop, as a potential source of food functional components.

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