| 波纹巴非蛤ACE抑制肽的分离纯化 |
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| 引用本文： | 曹文红,李岢斐.波纹巴非蛤ACE抑制肽的分离纯化[J].食品研究与开发,2011,32(10):134-138. |
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| 作者姓名： | 曹文红 李岢斐 |
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| 作者单位： | 广东海洋大学食品科技学院,广东湛江,524025 |
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| 基金项目： | 广东海洋大学自然科学团队项目(No.0612258) |
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| 摘 要： | 将波纹巴菲蛤酶解液经过凝胶层析柱(Sephadex G-15)分离收集到4个活性成分,活性最强的ACE抑制率达84.18%(0.5 mg/mL)。将组分4经过离子交换层析柱(SP Sephadex C-25)分离,并收集的高活性成分在可溶性蛋白为0.132 mg/mL ACE抑制率达到46.03%。最后将先后经过凝胶层析柱和离子交换层析柱收集到的ACE抑制率较高的组分通过反向高效液相色谱分析,出现2个洗脱峰,表明分离纯化效果良好。
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| 关 键 词： | 波纹巴菲蛤 酶解产物 血管紧张素转换酶抑制肽 分离纯化 |
Purification of ACE Inhibitory Peptides from the Enzymatic Hydrolysate of Paphia Undulate |
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| CAO Wen-hong,LI Ke-fei.Purification of ACE Inhibitory Peptides from the Enzymatic Hydrolysate of Paphia Undulate[J].Food Research and Developent,2011,32(10):134-138. |
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| Authors: | CAO Wen-hong LI Ke-fei |
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| Affiliation: | CAO Wen-hong,LI Ke-fei (College of Food Science and Technology,Guangdong Ocean University,Zhanjiang 524025,Guangdong,China) |
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| Abstract: | The enzymatic hydrolysate of Paphia undulata was flowed in a Sephadex G-15 column.Four fractions were collected and measured the ACE inhibitory activity.The result showed that the ACE inhibitory activity of fraction 4 was 84.18 % in a concentration of 0.5 mg/mL,which exerted the most active inhibitory activity.Fraction 4 was subjected to a SP Sephadex C-25 column to get further purification,and two fractions yielded.Fraction II showed an inhibition of 46.03 % at 0.132 mg/mL.Finally,fraction II was injected ... |
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| Keywords: | Paphia undulata enzymatic hydrolysate ACE inhibitory peptides purification |
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