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| Plastein reaction modification of pumpkin seed ACE inhibitory peptide and its isolation and identification |
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| DOI： |
| KeyWord:pumpkin seed ACE inhibitory peptide Plastein reaction isolation and identification |
| FundProject: |
| Author Name | Affiliation | | HU Tianyuan1, YANG Chen1, CHEN Zhe2,3, ZHENG Jingcheng1,3, HE Dongping1,3, YANG Yong2,3, LEI Fenfen1,3 | 1.College of Food Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, China
2.Wuhan Institute for Food and Cosmetic Control, Wuhan 430040, China
3.Key Laboratory of Edible Oil Quality and Safety for State Market Regulation，Wuhan 430040, China |
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| Abstract: |
| Plastein reaction was applied to modify pumpkin seed polypeptide to further enhance its ACE inhibitory activity. The effects of substrate mass fraction, reaction temperature, reaction time, and the addition of three exogenous amino acids on the inhibition rate of ACE inhibitory peptides were studied. The modified products were separated by ultrafiltration and Sephadex G-25 column chromatography, and were identified by LC-MS/MS. The results showed that the optimal conditions for Plastein reaction modification were substrate mass fraction 45%, reaction temperature 20℃, and reaction time 3 h. Adding leucine, phenylalanine or glycine respectively could significantly increase the ACE inhibition rate of the modified products. When 0.5 mmol/g leucine was added, the ACE inhibition rate of the modified product was up to 24.50 percentage points higher than that before the modification. After ultrafiltration and Sephadex G-25 column chromatography separation, the fraction with 89.61% ACE inhibition rate was obtained. A total of 76 peptides was identified by LC-MS/MS, and 4 of them with IFH, IFF, LAAF and DFHPR were synthesized by solid phase, and their IC50 for ACE inhibition were 1.55, 2.24, 3.79 mmol/L and 7.86 mmol/L, respectively. In summary, Plastein reaction can significantly improve the ACE inhibitory activity of pumpkin seed ACE inhibitory peptide, and the pumpkin seed ACE inhibitory peptide with high ACE inhibitory activity can be separated by ultrafiltration and Sephadex G-25 column chromatography. |
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