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| Structure characterization and performance determination of Porphyra yezoensis ACEI peptides |
| 1.School of Food and Biological Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China; 2.Jiangsu Key Laboratory for Physical Processing on Agricultural Products, Zhenjiang, Jiangsu 212013, China; 3.Jiangsu Province Research Center of Bioprocess and Separation of Agriproducts, Zhenjiang, Jiangsu 212013, China) |
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Abstract Angiotensin I converting enzyme inhibitory (ACEI) peptides extracted from Porphyra yezoensis protein were purified and identified. The stability and antihypertensive effect of peptides on spontaneously hypertensive rats were also investigated. After two-step reverse phase high performance liquid chromatography purification, two ACEI peptides were achieved and identified by liquid chromatography mass spectrometry analysis as Cys Ser Asn Arg and ProCysHisTrpw with 50% inhibitory concentration on Angiotensin I converting enzyme of 24.71 μmol·L-1 and 5.38 μmol·L-1, respectively. The results indicate that Porphyra yezoensis ACEI peptides are stable under neutral or acidic condition, but with poor resistance to high temperature. The significant antihypertensive effect of Porphyra yezoensis ACEI peptides (MW<3 ku fraction) on spontaneously hypertensive rats was observed in oral administration test, and the blood pressure of rats decreases obviouly with the increasing of dose.
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2012, Vol. 33 
