In vitro antioxidant activity of a peptide isolated from Nile tilapia (Oreochromis niloticus) scale gelatin in free radical-mediated oxidative systems

Ngo, Dai Hung; Qian, Zhong Ji; Ryu, BoMi; Park, Jae W.; Kim, Se‐Kwon

doi:10.1016/j.jff.2010.02.001

Cited by 174 publications

(80 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Other sources include meat, fish, eggs, plant sources such as soy and wheat (Hartmann and Meisel, 2007). The most commonly used enzymes for the production of bioactive peptides, for instance, from fish proteins include Alcalase 2.4 L FG, Papain, Pepsin, Trypsin, a-chymotrypsin, Pancreatin, Flavourzyme, Pronase, Neutrase, Protamex, Bromelain, Cryotin F, Protease N, Protease A, Orientase, Thermolysin, and Validase (Raghavan and Kristinsson, 2008;Ren et al, 2008;Samaranayaka and Li-chan, 2008;Je et al, 2009;Hsu, 2010;Ngo et al, 2010). Some of these enzymes are also used for production of bioactive peptides from other sources.…”

Section: Introductionmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

120

View full text Add to dashboard Cite

Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

show abstract

Section: Introductionmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

120

View full text Add to dashboard Cite

show abstract

“…For radical scavenging activity, the EC 50 of the peptide E1 was found to be the lowest (338 lg ml -1 ) among the four bioactive peptides obtained. It was lower than the peptides DPALA-TEPDPMPF (EC 50 = 660 lg ml -1 ) obtained from Nile tilapia scale gelatin [34], and RSGH-Pc, a cobia gelatin peptide (scavenging activity of 60.7 % at a concentration of 10 mg ml -1 ) [56]. At a concentration of 11 mg ml -1 , pepsin hydrolysate of porcine skin collagen had a radical scavenging [24].…”

Section: Identification and Characterization Of The Cryptic Peptidementioning

confidence: 78%

Isolation and Identification of Cryptic Bioactive Regions in Bovine Achilles Tendon Collagen

Banerjee¹,

Suseela²,

Shanthi³

2012

Protein J

View full text Add to dashboard Cite

Several proteins are known to host specific regions within their sequence, that when exposed or excised out proteolytically can display a range of physiological activities quite different from that of the parent protein. Collagen, a class of structural biopolymers and an important component of the extracellular matrix, is now known to harbor several such bioactive peptides which can act as physiological regulators. This study was undertaken to identify such cryptic sites from bovine Achilles tendon collagen and an antioxidative assay was used to screen for bioactivity. Bacterial crude protease was used to hydrolyze collagen and the hydrolysate was subjected to separation through ion-exchange column chromatography. Fractions were screened using conventional antioxidative assays and further purified by gel permeation chromatography. Two biologically active cryptic peptides were obtained displaying high antioxidative properties, E1 and F3. At low concentrations, both peptides displayed higher chelating ability than EDTA and were able to reduce the auto-oxidation of unsaturated fatty acid. The molecular weights of the peptides were found out through column chromatography and Tricine SDS PAGE; both displayed molecular mass below 4 kDa. Overall E1 displayed a comparatively better antioxidative ability than the others and was further characterized by circular dichroism studies and sequencing. A BLAST search of the active peptide sequence revealed that an almost similar peptide also resides in human collagen Type I.

show abstract

“…Recently, protein hydrolysates obtained by enzymatic digestion of various marine resources tuna liver (Je et al 2009), pink perch (Shabeena and Nazeer 2010), nile tilapia (Ngo et al 2010), gastropod (Nazeer and Srividhya 2011) and sea urchin (Qin et al 2011) were reported to have antioxidant activity. In the present study viscera and foot were chosen and processed further for hydrolysis using commercial enzymes (pepsin, trypsin and papain) and the prepared hydrolysates were evaluated for their antioxidant activity using DPPH radical scavenging activity and reducing power ability assay.…”

Section: Preparation Of Clam Protein Hydrolysates and Their Antioxidamentioning

confidence: 99%

Radical scavenging and amino acid profiling of wedge clam, Donax cuneatus (Linnaeus) protein hydrolysates

2012

View full text Add to dashboard Cite

Body, foot and viscera of Donax cuneatus (Linnaeus) were hydrolyzed using commercial proteases (pepsin, trypsin and papain) and tested for their antioxidant activity by DPPH scavenging ability and reducing power assays. In comparison between all the hydrolysates, papain viscera (28.513±0.165 & 0.186±0.008) and foot (33.567± 0.132 & 0.166±0.013) hydrolysates showed highest DPPH and reducing power ability respectively. The active hydrolysates were purified with DEAE-cellulose followed by Sephadex G-25 columns connected to FPLC. Further, the isolated active fractions were loaded onto HPLC for their amino acid profiling and found with the presence of potential amino acids viz., histidine, cysteine, alanine etc. These results suggest that the isolated antioxidant peptide from viscera and foot hydrolysate of D. cuneatus can be used in treating human diseases where free radicals and oxidative damage are involved.

show abstract

In vitro antioxidant activity of a peptide isolated from Nile tilapia (Oreochromis niloticus) scale gelatin in free radical-mediated oxidative systems

Cited by 174 publications

References 37 publications

Peptides: Production, bioactivity, functionality, and applications

Peptides: Production, bioactivity, functionality, and applications

Isolation and Identification of Cryptic Bioactive Regions in Bovine Achilles Tendon Collagen

Radical scavenging and amino acid profiling of wedge clam, Donax cuneatus (Linnaeus) protein hydrolysates

Contact Info

Product

Resources

About