2016
DOI: 10.1080/10942912.2016.1160409
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Purification and antioxidant ability of peptide from egg in sea cucumberApostichopus japonicus

Abstract: The antioxidant peptide was prepared from hydrolyzed egg of Apostichopus japonicus. Ultra-filtration, high-speed counter-current chromatography and gel filtration were used in peptide purification. In each step of purification, meanwhile, peptide was tested with its antioxidant ability. The purity and molecular weight was tested by using Tricine-sodium dodecyl sulphatepolyacrylamide gel electrophoresis. Results showed that the purified peptide obtained a sharply enhancing ability to scavenge hydroxyl radical f… Show more

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Cited by 9 publications
(11 citation statements)
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“…[34] The next most potent antioxidative peptide was Peptide 3 (PGRRAA), followed by Peptide 2 (PTPSRPQQGPA), and the results were similar to those in previous reports on antioxidant peptides isolated from fish by-products with EC 50 values from 90 to 670 mM, [57,58] peptide derived from horse mackerel viscera proteolysate with DPPH • radical scavenging activity of 59.1%, [30] and the antioxidative peptides derived from sardinelle with the DPPH • radical scavenging activity from 38 ± 1.3% to 63 ± 1.5%, [20] but were lower than Apostichopus japonicas egg proteolysates with hydroxyl radical scavenging activity of 89.82 U/mL. [59] Peptide 4 (LAQVAVSNPNN) showed negative ABTS • (−19% at 5 mg/mL) and DPPH • (−34% at 5 mg/mL) radical scavenging values, suggesting that the peptide has pro-oxidant activity. A similar argument was proposed by Shen et al (2010) [60] for two peptides (LSKAQSDFG) and (LVEKGDVAFI) originating from ovotransferrin, which were shown to have negative antioxidant activity.…”
Section: Peptide Identificationmentioning
confidence: 89%
“…[34] The next most potent antioxidative peptide was Peptide 3 (PGRRAA), followed by Peptide 2 (PTPSRPQQGPA), and the results were similar to those in previous reports on antioxidant peptides isolated from fish by-products with EC 50 values from 90 to 670 mM, [57,58] peptide derived from horse mackerel viscera proteolysate with DPPH • radical scavenging activity of 59.1%, [30] and the antioxidative peptides derived from sardinelle with the DPPH • radical scavenging activity from 38 ± 1.3% to 63 ± 1.5%, [20] but were lower than Apostichopus japonicas egg proteolysates with hydroxyl radical scavenging activity of 89.82 U/mL. [59] Peptide 4 (LAQVAVSNPNN) showed negative ABTS • (−19% at 5 mg/mL) and DPPH • (−34% at 5 mg/mL) radical scavenging values, suggesting that the peptide has pro-oxidant activity. A similar argument was proposed by Shen et al (2010) [60] for two peptides (LSKAQSDFG) and (LVEKGDVAFI) originating from ovotransferrin, which were shown to have negative antioxidant activity.…”
Section: Peptide Identificationmentioning
confidence: 89%
“…The multi-enzyme hydrolysis process is mainly divided into biphase sequential enzymolysis mode, two-step enzymolysis mode and their combined method [80]. Zhang et al used a mixed enzyme (Papain:Protamex = 1:1) and Flavorzyme to hydrolyze egg extract in sea cucumber (Apostichopus japonicus) step by step, and gradually purified the hydrolysate [62]. Finally, a pure PA (Mw: about 30 kDa) with a high • OH scavenging capacity of 89.82 U/mL was obtained.…”
Section: Sourcementioning
confidence: 99%
“…Therefore, enzymatic digestion of protein has been the most common method for preparation of antioxidant peptides due to the simplicity, safety, low-cost, and sustainability of the approach [8]. Collagen is an important structural protein rich in hydroxyproline, which has been employed in food and medical applications for decades with excellent biocompatibility and safety [9,10]. For example, the collagens from echinoderms (sea urchin, starfish, and sea cucumber) can be used to develop collagen barrier-membranes for guided tissue regeneration due to the good mechanical performances [11].…”
Section: Introductionmentioning
confidence: 99%