Purification and identification of Se-containing antioxidative peptides from enzymatic hydrolysates of Se-enriched brown rice protein

Liu, Kunlun; Zhao, Yan; Chen, Fusheng; Fang, Yong

doi:10.1016/j.foodchem.2015.04.086

Cited by 57 publications

(42 citation statements)

References 31 publications

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“…Peptides with basic and/or hydrophobic amino acid residues, such as His, Lys and Pro, are thought to have strong antioxidant activities [24]. Therefore, anion and cation exchange resins have been widely used to purify antioxidant peptides from protein hydrolysates [25,26,27]. The present data showed that Fr.4 had the strongest HO• scavenging activity and was selected for further purification.…”

Section: Resultsmentioning

confidence: 90%

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: 90%

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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“…We found that rice-derived peptides increased intracellular glutathione levels. Rice is widely consumed around the world and rice-derived peptides are reported to have various biological effects such as anti-microbial activity, (8,9) anti-oxidative activity (10,11) and dipeptidyl peptidase-IV-inhibitory activity. (12,13) Compounds that have so far been reported to increase intracellular glutathione levels include silymarin, (14) cyanohydroxybutene, (15) α-naphthoflavone, (16) apocynin, (17) epalrestat, (18,19) ribose-cysteine, (20) β-carotene, (21) noradrenaline, (22) and lactacystin.…”

Section: Introductionmentioning

confidence: 99%

Hepatoprotective effects of rice-derived peptides against acetaminophen-induced damage in mice

Kawakami

Moritani

Uraji³

et al. 2017

J. Clin. Biochem. Nutr.

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Glutathione, the most abundant intracellular antioxidant, protects cells against reactive oxygen species induced oxidative stress and regulates intracellular redox status. We found that rice peptides increased intracellular glutathione levels in human hepatoblastoma HepG2 cells. Acetaminophen is a commonly used analgesic. However, an overdose of acetaminophen causes severe hepatotoxicity via depletion of hepatic glutathione. Here, we investigated the protective effects of rice peptides on acetaminophen-induced hepatotoxicity in mice. ICR mice were orally administered rice peptides (0, 100 or 500 mg/kg) for seven days, followed by the induction of hepatotoxicity via intraperitoneal injection of acetaminophen (700 mg/kg). Pretreatment with rice peptides significantly prevented increases in serum alanine aminotransferase, aspartate aminotransferase, and lactate dehydrogenase levels and protected against hepatic glutathione depletion. The expression of γ-glutamylcysteine synthetase, a key regulatory enzyme in the synthesis of glutathione, was decreased by treatment with acetaminophen, albeit rice peptides treatment recovered its expression compared to that achieved treatment with acetaminophen. In addition, histopathological evaluation of the livers also revealed that rice peptides prevented acetaminophen-induced centrilobular necrosis. These results suggest that rice peptides increased intracellular glutathione levels and could protect against acetaminophen-induced hepatotoxicity in mice.

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“…Ion‐exchange chromatography (PuriFlash 450, Interchim, France) was applied to separate and purify ultrafiltration products with high antigenicity (Jungbauer & Hahn, ; Liu, Zhao, Chen, & Fang, ). The freeze‐dried ultrafiltration products were dissolved in deionized water and then loaded onto a diethylaminoethyl cellulose (DEAE) Sepharose Fast Flow (FF) column (1.5 cm × 46 cm) equilibrated by 20 mmol/L of Tris–HCl buffer (pH 8.0).…”

Section: Methodsmentioning

confidence: 99%

“…Ion-exchange chromatography (PuriFlash 450, Interchim, France) was applied to separate and purify ultrafiltration products with high antigenicity (Jungbauer & Hahn, 2009;Liu, Zhao, Chen, & Fang, 2015). The freeze-dried ultrafiltration products were dissolved in deionized water and then loaded onto a diethyl-…”

Section: Purification Of Ultrafiltration Productmentioning

confidence: 99%

The separation and identification of the residual antigenic fragments in soy protein hydrolysates

Huang

2020

J Food Biochem

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Soybean is one of the major food allergens. In this study, soy protein isolate was hydrolyzed by Neutrase and Flavourzyme. The hydrolysates were separated by ultrafiltration and ion‐exchange chromatography. The antigenicity of proteins was determined by indirect competitive ELISA. The molecular weight distribution was characterized by SDS–PAGE. The amino acid sequence of chromatography fractions was analyzed by LC‐MS. The results showed that proteins with >50 kDa in hydrolysates had the highest antigenicity and were further separated into F1–F5 fragments by ion‐exchange chromatography. Fragment F4, which was the most antigenic, was analyzed by LC‐MS. The results of mass spectrometry showed that most of the peptides that contained antigen epitopes in chromatography fraction F4 belonged to glycinin subunits. The antigenicity of soy protein was reduced by enzymatic hydrolysis, but glycinin showed resistance to enzymatic hydrolysis. Practical applications The identification of residual antigenicity in soy protein hydrolysates by LC‐MS provides important information on the resistance mechanism of enzymatic hydrolysis of soybean protein allergens. In addition, the efficient separation of soy protein hydrolysates could be beneficial for developing low‐allergenic soybean products.

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Purification and identification of Se-containing antioxidative peptides from enzymatic hydrolysates of Se-enriched brown rice protein

Cited by 57 publications

References 31 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

Hepatoprotective effects of rice-derived peptides against acetaminophen-induced damage in mice

The separation and identification of the residual antigenic fragments in soy protein hydrolysates

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