Influence of degree of hydrolysis on functional properties, antioxidant and ACE inhibitory activities of egg white protein hydrolysate

Chen, Chen; Chi, Yujie; Zhao, Ming-Yang; Xu, Wei

doi:10.1007/s10068-012-0004-6

Cited by 70 publications

(60 citation statements)

References 30 publications

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“…Chen et al (2012) reported that the Gly residue may contribute significantly to antioxidant activity since the single hydrogen atom in the side chain of Gly serves as a proton-donating source and neutralizes active free radical species [44]. In addition, Nimalaratne et al (2015) reported that the single hydrogen atom of Gly (G) can provide high flexibility to the peptide backbone and positively influence the antioxidant properties [8].…”

Section: Resultsmentioning

confidence: 99%

Purification and Identification of Antioxidant Peptides from Protein Hydrolysate of Scalloped Hammerhead (Sphyrna lewini) Cartilage

Chi

et al. 2017

Marine Drugs

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The aim of this study was to purify and identify peptides with antioxidant properties from protein hydrolysate of scalloped hammerhead (Sphyrna lewini) cartilage. Cartilaginous proteins of the scalloped hammerhead were extracted by guanidine hydrochloride, and three antioxidant peptides, named enzymolysis peptide of scalloped hammerhead cartilage A (SCPE-A), SCPE-B and SCPE-C, were subsequently isolated from the hydrolysate of the cartilaginous proteins using ultrafiltration and chromatography. The amino acid sequences of SCPE-A, SCPE-B and SCPE-C were identified as Gly-Pro-Glu (GPE), Gly-Ala-Arg-Gly-Pro-Gln (GARGPQ), and Gly-Phe-Thr-Gly-Pro-Pro-Gly-Phe-Asn-Gly (GFTGPPGFNG), with molecular weights of 301.30 Da, 584.64 Da and 950.03 Da, respectively. As per in vitro activity testing, SCPE-A, SCPE-B and SCPE-C exhibited strong scavenging activities on 2,2-diphenyl-1-picrylhydrazyl radicals (DPPH•) (half elimination ratio (EC50) 2.43, 2.66 and 1.99 mg/mL), hydroxyl radicals (HO•) (EC50 0.28, 0.21 and 0.15 mg/mL), 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid radicals (ABTS+•) (EC50 0.24, 0.18 and 0.29 mg/mL), and superoxide anion radicals (normalO2−•) (EC50 0.10, 0.14 and 0.11 mg/mL). In addition, SCPE-A showed inhibition activity similar to butylated hydroxytoluene (BHT) in lipid peroxidation in a linoleic acid model system. The amino acid residues of Gly, Pro and Phe could positively influence the antioxidant activities of GPE, GARGPQ and GFTGPPGFNG. These results suggested that GPE, GARGPQ and GFTGPPGFNG might serve as potential antioxidants and be used as food additives and functional foods.

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Section: Resultsmentioning

confidence: 99%

Purification and Identification of Antioxidant Peptides from Protein Hydrolysate of Scalloped Hammerhead (Sphyrna lewini) Cartilage

Chi

et al. 2017

Marine Drugs

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“…Gly residue may contribute significantly to antioxidant activity since the single hydrogen atom in the side chain of Gly serves as protons-donating and neutralises active free radical species (Chen, Chi, Zhao, & Xu, 2012) .…”

Section: Discussionmentioning

confidence: 99%

Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysate

Mirzaei

Mirdamadi

Ehsani

et al. 2015

Journal of Functional Foods

105

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Available online A B S T R A C TYeast protein hydrolysate may be considered as a good source of bioactive peptides. Yeast hydrolysate was prepared by two different physical-enzymatic and autolysis treatments to identify the most active angiotensin I-converting enzyme (ACE) inhibitory and antioxidant peptides. The most active hydrolysate was obtained after sonication-trypsin hydrolysis. The hydrolysate was subjected to fractionation by ultrafiltration. Fraction with molecular weight of <3 kDa exhibited the highest activity. Reverse phase high performance liquid chromatography (RP-HPLC) resolved this fraction into five fractions, one of which (fraction F3) with amino acid sequence of Tyr-Gly-Lys-Pro-Val-Ala-Val-Pro-Ala-Arg (MW:1057.45 Da) exhibited ACE inhibitory (IC50 = 0.42 ± 0.02 mg/ml) and antioxidant activities (26.25 ± 0.13 µM TE/µg protein). Taken together, the results of this study show that S. cerevisiae proteins contain specific peptides in their sequences which can be released by enzymatic hydrolysis. These peptides have excellent bioactive properties that can potentially replace the antioxidant and antihypertensive agents with chemical origin.

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“…The amino acid sequence of the peptide might play an important role in its activity [9]. Other papers that studied the antioxidant of protein hydrolysates reported that the molecular weight of hydrolysates ranged from 551 Da up to 3 k Da [10][11][12] …”

Section: -4mentioning

confidence: 99%

Novel source of protein extract from nyamplung (Calophyllum inophyllum)

Yanti¹,

Hastuti²,

Sulistyo³

et al. 2016

AIP Conference Proceedings

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Influence of degree of hydrolysis on functional properties, antioxidant and ACE inhibitory activities of egg white protein hydrolysate

Cited by 70 publications

References 30 publications

Purification and Identification of Antioxidant Peptides from Protein Hydrolysate of Scalloped Hammerhead (Sphyrna lewini) Cartilage

Purification and Identification of Antioxidant Peptides from Protein Hydrolysate of Scalloped Hammerhead (Sphyrna lewini) Cartilage

Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysate

Novel source of protein extract from nyamplung (Calophyllum inophyllum)

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