Journal
MOLECULES
Volume 24, Issue 10, Pages -Publisher
MDPI
DOI: 10.3390/molecules24101946
Keywords
pacific herring; protein hydrolysate; peptides; antioxidant activity; purification
Funding
- Key Research and Development Program of Shandong Province [2017YYSP018]
- STS Project of the Chinese Academy of Sciences [2017T3006]
- Qingdao Science and Technology Project [17-3-3-21-nsh]
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The aim of this study was to isolate and purify antioxidative peptides from Pacific herring (Clupea pallasii) protein. Five enzymes (pepsin, trypsin, papain, flavourzyme, and neutrase) were used for protein hydrolysis, and Pacific herring protein hydrolysates (PHPH) were separated by ultrafiltration. The fraction with the molecular weight below 3500 Da exhibited the highest in vitro antioxidant activities and cellular antioxidant activity. The PHPH was isolated and purified by consecutive chromatographic methods including gel filtration chromatography and reverse high-performance liquid chromatography (RP-HPLC). The purified antioxidant peptides were identified as Leu-His-Asp-Glu-Leu-Thr (MW = 726.35 Da) and Lys-Glu-Glu-Lys-Phe-Glu (MW = 808.40 Da), and the IC50 values of cellular antioxidant activity were 1.19 +/- 0.05 mg/mL and 1.04 +/- 0.06 mg/mL. The results demonstrate that is possible to produce natural antioxidative peptides from Pacific herring protein via enzymatic hydrolysis and purification.
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