Preparation and Identification of Antioxidative Peptides from Pacific Herring (<i>Clupea pallasii</i>) Protein
The aim of this study was to isolate and purify antioxidative peptides from Pacific herring (<i>Clupea pallasii</i>) protein. Five enzymes (pepsin, trypsin, papain, flavourzyme, and neutrase) were used for protein hydrolysis, and Pacific herring protein hydrolysates (PHPH) were separated...
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| Format: | Article |
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MDPI AG
2019-05-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/24/10/1946 |
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| author | Xueqin Wang Huahua Yu Ronge Xing Song Liu Xiaolin Chen Pengcheng Li |
| author_facet | Xueqin Wang Huahua Yu Ronge Xing Song Liu Xiaolin Chen Pengcheng Li |
| author_sort | Xueqin Wang |
| collection | DOAJ |
| description | The aim of this study was to isolate and purify antioxidative peptides from Pacific herring (<i>Clupea pallasii</i>) 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 IC<sub>50</sub> 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. |
| first_indexed | 2024-12-11T21:03:55Z |
| format | Article |
| id | doaj.art-1f617a7b5cfa4762b4024c94245ca67f |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-11T21:03:55Z |
| publishDate | 2019-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-1f617a7b5cfa4762b4024c94245ca67f2022-12-22T00:50:55ZengMDPI AGMolecules1420-30492019-05-012410194610.3390/molecules24101946molecules24101946Preparation and Identification of Antioxidative Peptides from Pacific Herring (<i>Clupea pallasii</i>) ProteinXueqin Wang0Huahua Yu1Ronge Xing2Song Liu3Xiaolin Chen4Pengcheng Li5Key Laboratory of Experimental Marine Biology, Center for Ocean Mega-Science, Institute of Oceanology, Chinese Academy of Sciences, No 7, Nanhai Road, Qingdao 266071, ChinaKey Laboratory of Experimental Marine Biology, Center for Ocean Mega-Science, Institute of Oceanology, Chinese Academy of Sciences, No 7, Nanhai Road, Qingdao 266071, ChinaKey Laboratory of Experimental Marine Biology, Center for Ocean Mega-Science, Institute of Oceanology, Chinese Academy of Sciences, No 7, Nanhai Road, Qingdao 266071, ChinaKey Laboratory of Experimental Marine Biology, Center for Ocean Mega-Science, Institute of Oceanology, Chinese Academy of Sciences, No 7, Nanhai Road, Qingdao 266071, ChinaKey Laboratory of Experimental Marine Biology, Center for Ocean Mega-Science, Institute of Oceanology, Chinese Academy of Sciences, No 7, Nanhai Road, Qingdao 266071, ChinaKey Laboratory of Experimental Marine Biology, Center for Ocean Mega-Science, Institute of Oceanology, Chinese Academy of Sciences, No 7, Nanhai Road, Qingdao 266071, ChinaThe aim of this study was to isolate and purify antioxidative peptides from Pacific herring (<i>Clupea pallasii</i>) 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 IC<sub>50</sub> 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.https://www.mdpi.com/1420-3049/24/10/1946pacific herringprotein hydrolysatepeptidesantioxidant activitypurification |
| spellingShingle | Xueqin Wang Huahua Yu Ronge Xing Song Liu Xiaolin Chen Pengcheng Li Preparation and Identification of Antioxidative Peptides from Pacific Herring (<i>Clupea pallasii</i>) Protein Molecules pacific herring protein hydrolysate peptides antioxidant activity purification |
| title | Preparation and Identification of Antioxidative Peptides from Pacific Herring (<i>Clupea pallasii</i>) Protein |
| title_full | Preparation and Identification of Antioxidative Peptides from Pacific Herring (<i>Clupea pallasii</i>) Protein |
| title_fullStr | Preparation and Identification of Antioxidative Peptides from Pacific Herring (<i>Clupea pallasii</i>) Protein |
| title_full_unstemmed | Preparation and Identification of Antioxidative Peptides from Pacific Herring (<i>Clupea pallasii</i>) Protein |
| title_short | Preparation and Identification of Antioxidative Peptides from Pacific Herring (<i>Clupea pallasii</i>) Protein |
| title_sort | preparation and identification of antioxidative peptides from pacific herring i clupea pallasii i protein |
| topic | pacific herring protein hydrolysate peptides antioxidant activity purification |
| url | https://www.mdpi.com/1420-3049/24/10/1946 |
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