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J Microbiol Biotechnol. 2016 Jul 28;26(7):1216-23. doi: 10.4014/jmb.1601.01033.

Purification and Identification of Antioxidant Peptides from Enzymatic Hydrolysate of Spirulina platensis.

Yu J1,2, Hu Y1,2, Xue M3, Dun Y2, Li S2, Peng N2, Liang Y2,4, Zhao S2,4.

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Hubei Key Laboratory of Edible Wild Plants Conservation & Utilization, College of Life Sciences, Hubei Normal University, Huangshi 435002, P.R. China.
State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, P.R. China.
Beihai Shengbada Biotech Co., Ltd, Beihai 536000, P.R. China.
Hubei Collaborative Innovation Center for Industrial Fermentation, Wuhan 430068, P.R. China.


The aim of this study was to isolate antioxidant peptides from an enzymatic hydrolysate of Spirulina platensis. A novel antioxidant peptide was obtained by ultrafiltration, gel filtration chromatography, and reverse-phase high-performance liquid chromatography, with the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging assay used to measure the antioxidant activity, and the sequence was determined to be Pro-Asn-Asn (343.15 Da) by electrospray ionization tandem mass spectrometry. This peptide was synthesized to confirm its antioxidant properties, and it exhibited 81.44 ± 0.43% DPPH scavenging activity at 100 µg/ml, which was similar to that of glutathione (82.63 ± 0.56%). Furthermore, the superoxide anion and hydroxyl free-radical scavenging activities and the SOD activity of the peptide were 47.84 ± 0.49%, 54.01 ± 0.82%, and 12.55 ± 0.75%, respectively, at 10 mg/ml. These results indicate that S. platensis is a good source of antioxidant peptides, and that its hydrolysate may have important applications in the pharmaceutical and food industries.


Antioxidant peptide; Spirulina platensis; free-radical scavenging activity; mass spectrometry; purification

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