Preparation and Identification of Antioxidative Peptides from Pacific Herring (Clupea pallasii) Protein

被引:33
|
作者
Wang, Xueqin [1 ,2 ]
Yu, Huahua [1 ,2 ]
Xing, Ronge [1 ,2 ]
Liu, Song [1 ,2 ]
Chen, Xiaolin [1 ,2 ]
Li, Pengcheng [1 ,2 ]
机构
[1] Chinese Acad Sci, Key Lab Expt Marine Biol, Ctr Ocean Mega Sci, Inst Oceanol, 7 Nanhai Rd, Qingdao 266071, Shandong, Peoples R China
[2] Qingdao Natl Lab Marine Sci & Technol, Lab Marine Drugs & Bioprod, 1 Wenhai Rd, Qingdao 266237, Shandong, Peoples R China
关键词
pacific herring; protein hydrolysate; peptides; antioxidant activity; purification; RAPANA-VENOSA MEAT; RESPONSE-SURFACE; HEPG2; CELLS; IN-VITRO; VISCERAL MASS; AMINO-ACID; PURIFICATION; OPTIMIZATION; HYDROLYSATE; MUSCLE;
D O I
10.3390/molecules24101946
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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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页数:17
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