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Molecules 2017, 22(1), 57; doi:10.3390/molecules22010057

Purification and Characterization of Antioxidant Peptides of Pseudosciaena crocea Protein Hydrolysates

1
College of Food Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China
2
Fuzhou Municipal Finance Office, Fuzhou 350002, China
*
Author to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 12 November 2016 / Revised: 28 December 2016 / Accepted: 29 December 2016 / Published: 30 December 2016
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Abstract

Two peptides with antioxidant activity were isolated from Pseudosciaena crocea proteins. Pseudosciaena crocea muscle was hydrolyzed with neutral protease to obtain Pseudosciaena crocea protein hydrolysates (PCPH). After ultrafiltration through molecular weight cut-off membranes of 10, 5 and 3 kDa and assessment of free radical scavenging ability, the fraction (PCPH-IV) with the highest antioxidant activity was obtained. Several purification steps, i.e., ion exchange chromatography, gel filtration chromatography and reversed phase high performance liquid chromatography, were applied to further purify PCPH-IV. Two antioxidant peptides with the amino acid sequences Ser-Arg-Cys-His-Val and Pro-Glu-His-Trp were finally identified by LC-MS/MS. View Full-Text
Keywords: Pseudosciaena crocea; antioxidant; peptide purification; chromatographic separation; amino acid sequence Pseudosciaena crocea; antioxidant; peptide purification; chromatographic separation; amino acid sequence
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Zhang, N.; Zhang, C.; Chen, Y.; Zheng, B. Purification and Characterization of Antioxidant Peptides of Pseudosciaena crocea Protein Hydrolysates. Molecules 2017, 22, 57.

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