An antioxidant peptide derived from Ostrich (Struthio camelus) egg white protein hydrolysates

Tanzadehpanah, Hamid; Asoodeh, Ahmad; Chamani, Jamshidkhan

doi:10.1016/j.foodres.2012.08.022

Cited by 85 publications

(48 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…On the other hand, it has been reported that the presence of hydrophobic amino acids and one or more residues of H, P, C, Y, W, F, or M, might improve the antioxidant activity in peptides [48], especially the amino acid His which is reportedly important to the antioxidant activity of peptides for its imidazole characteristics that indicate protondonation capability [49]. In this respect, peptides GPAGFA and GEPGAP from S3 were synthesized and tested for its antioxidant activity.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Bioactive peptides identified in thornback ray skin's gelatin hydrolysates by proteases from Bacillus subtilis and Bacillus amyloliquefaciens

Lassoued

Mora

Barkia

et al. 2015

Journal of Proteomics

105

View full text Add to dashboard Cite

Section: Accepted Manuscriptmentioning

confidence: 99%

Bioactive peptides identified in thornback ray skin's gelatin hydrolysates by proteases from Bacillus subtilis and Bacillus amyloliquefaciens

Lassoued

Mora

Barkia

et al. 2015

Journal of Proteomics

105

View full text Add to dashboard Cite

“…Wattanasiritham, Theerakulkait, and Wickramasekara () suggest peptides that contain P, G, A, V, and L in the peptide sequences have intrinsic antioxidant activity. Tanzadehpanah, Asoodeh, and Chamani () suggested that hydrophobic residues (V, L, I, A, F, and K) at the C‐termini or N ‐termini contribute to the antioxidant activity of the peptides. Li and Li () suggest bulky hydrophobic amino acid with low electronic or steric/hydrogen bonding properties, such as W, Y, F, M, L, and I at the third position of the amino acid next to the C‐terminus, contribute to the antioxidant activity.…”

Section: Resultsmentioning

confidence: 99%

Identification and analysis of bioactive peptides from scallops (Chlamys farreri ) protein by simulated gastrointestinal digestion

et al. 2018

J Food Process Preserv

View full text Add to dashboard Cite

In this study, the hydrolysates of scallops (Chlamys farreri) protein were prepared by in vitro simulated gastrointestinal digestion. Antioxidant peptides, VPSIDDQEELM, DAQEKLE, EELDNALN, VPSIDDQEELM, DAQEKLE, EELDNALN, VPSIDDQEELM and VPSIDDQEELM, were identified by ultra performance liquid chromatography system coupled to a Synapt Mass Quadrupole Time‐of‐Flight Mass Spectrometer (UPLC‐Q‐TOF‐MS). The antioxidant activities of the CFP hydrolysates, i.e., reducing powers, linoleic acid peroxidation inhibition activity and 2, 2‐dipheny l‐1‐picrylhydrazyl (DPPH) free radical scavenging activities, were tested. The antioxidant activities (54.44% ± 0.02%), reducing power (0.250 ± 0.02) and DPPH free radical scavenging activities of the hydrolysates shows higher than the same concentration of protein solution. This research provided a theoretical and practical data for the application of the bioactive peptides form CFP. Practical applications In this research, what we focused on is the qualitative of peptides from the digestive solutions. It makes more sense to discuss about the information of the special analogues, sequence and activity of peptides from hydrolysis fragment after simulated gastrointestinal digestion of CFP. These peptides which have hydrophobic residues at the C‐termini contribute to the antioxidant activity of the peptides. Comparing the antioxidant activities of the same concentration of CFP solution and in vitro gastric and gastro duodenal digestion hydrolysates, the hydrolysates of the digestion had higher reducing powers, linoleic acid peroxidation inhibition activity, and DPPH free radical scavenging activities. It could be speculated that both the peptides at approximately low‐molecular‐mass peptides (10–15 kDa) were contributing to the antioxidant activities of the hydrolysates. After the target peptides were determined, the quantitative of peptides may be more meaningful. Quantitative calculation of the digestion will be clarified in future work.

show abstract

“…The inhibition of linoleic acid oxidation was measured using the method of Tanzadehpanah et al (2012), which was modified as follows. Briefly, 1.0 ml of sample (dissolved in 50 mM sodium phosphate buffer, pH 7.0) was mixed with 0.5 ml of distilled water and 1.0 ml of 50 mM linoleic acid in 95% ethanol.…”

Section: Methodsmentioning

confidence: 99%

Antioxidant activities of peptide fractions derived from freshwater mussel protein using ultrasound-assisted enzymatic hydrolysis

Zhouyong¹,

Tian²,

Xu³

et al. 2017

Czech J. Food Sci.

View full text Add to dashboard Cite

Dong Z., Tian G., Xu Z., Li M., Xu M., Zhou Y., Ren H. (2017): Antioxidant activities of peptide fractions derived from freshwater mussel protein using ultrasound-assisted enzymatic hydrolysis. Czech J. Food Sci., 35: 328-338.The freshwater mussel protein was hydrolysed using ultrasound-assisted enzymolysis. Ultrasound-assisted freshwater mussel protein hydrolysates (UPH) were divided into four fractions (> 10, 6-10, 3-6, and < 3 kDa) using ultrafiltration, and the fraction with the highest antioxidant activity was further subdivided into four fractions (F 1 -F 4 ) using gel chromatography. The amino acid compositions and antioxidant activities (DPPH, hydroxyl and superoxide radical scavenging activities, reducing power, ferrous ion chelating activity, and inhibition of linoleic acid oxidation) of peptide fractions were investigated. The results showed that the antioxidant activity of the < 3 kDa fraction was significantly higher than that of UPH, > 10, 6-10, and 3-6 kDa fractions. The antioxidant activity of F 2 was again higher compared with the < 3 kDa fraction and higher than that of F 1 , F 3 , and F 4 . Amino acid analysis showed that the antioxidant activities (except for chelating activity) of peptides increased with increasing hydrophobic amino acid content. The < 3 kDa and F 2 fractions exhibited strong inhibition of linoleic acid oxidation, their effects being even better than that of ascorbic acid (Vc) and l-glutathione (GSH). Therefore, these peptide fractions from freshwater mussel may be a potential natural antioxidant that could be added to various foods.

show abstract

An antioxidant peptide derived from Ostrich (Struthio camelus) egg white protein hydrolysates

Cited by 85 publications

References 35 publications

Bioactive peptides identified in thornback ray skin's gelatin hydrolysates by proteases from Bacillus subtilis and Bacillus amyloliquefaciens

Bioactive peptides identified in thornback ray skin's gelatin hydrolysates by proteases from Bacillus subtilis and Bacillus amyloliquefaciens

Identification and analysis of bioactive peptides from scallops (Chlamys farreri ) protein by simulated gastrointestinal digestion

Antioxidant activities of peptide fractions derived from freshwater mussel protein using ultrasound-assisted enzymatic hydrolysis

Contact Info

Product

Resources

About