Isolation and Identification of Angiotensin I-converting Enzyme Inhibitory Peptide Derived from Peptic Globin Hydrolysate by HPLC-ESI-MS

Abstract

Abstract: This paper described isolation and identification of angiotensin I-converting enzyme (ACE) inhibitory peptide derived from the peptic globin hydrolysate. After the isolation of ACE inhibitory peptide with reversed-phase high-perfor-mance liquid chromatography (RP-HPLC) on C18 column, one active fraction was obtained. The amino acid sequence was identified by electrospray ionization tandem mass spectrometry (ESI-MS-MS). The results showed that this peptide is Val-Val-Tyr-Pro-Trp-Thr(VVYPWT), corresponding to the 34-39 fragment of the β chain of porcine hemoglobin, with IC50 value as 6.02μmol/L.K e y w o r d s :RP-HPLC;MS;globin;VVYPWT

Key words: RP-HPLC, MS, globin, VVYPWT

YU Yi-Ke, HU Jian-恩, BAI Xue-Fang, DU Yu-Guang, LIN Bing-Cheng. Isolation and Identification of Angiotensin I-converting Enzyme Inhibitory Peptide Derived from Peptic Globin Hydrolysate by HPLC-ESI-MS[J]. FOOD SCIENCE, 2007, 28(12): 248-250.

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Isolation and Identification of Angiotensin I-converting Enzyme Inhibitory Peptide Derived from Peptic Globin Hydrolysate by HPLC-ESI-MS

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