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Purification and characterization of angiotensin I converting enzyme inhibition peptides from sandworm Sipunculus nudus

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Abstract

Three angiotensin I converting enzyme (ACE) inhibition peptides were isolated from sandworm Sipunculus nudus protein hydrolysate prepared using protamex. Consecutive purification methods, including size exclusion chromatography and reverse-phase high performance liquid chromatography (RP-HPLC), were used to isolate the ACE inhibition peptides. The amino acid sequences of the peptides were identified as Ile-Asn-Asp, Val-Glu-Pro-Gly and Leu-Ala-Asp-Glu-Phe. The IC50 values of the purified peptides for ACE inhibition activity were 34.72 μmol L−1, 20.55 μmol L−1 and 22.77 μmol L−1, respectively. These results suggested that S. nudus proteins contain specific peptides that can be released by enzymatic hydrolysis. This study may provide an experimental basis for further systematic research, rational development and clinical utilization of sandworm resources.

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Acknowledgements

This work is supported by research grant of Guangxi Key Laboratory Traditional Chinese Medicine Quality Standards (No. GXGZZK201501) and the Open Research Fund Program of Guangxi Key Laboratory of Marine Biotechnology (No. GLMBT-201407), and partly supported by Shanghai Fengxian District Science and Technology Project (Nos. 20141001 and 20151205), Shanghai No. 6 People’s Medical Group Project and research project of Shanghai municipal health and Family Planning Commission (No. 201540027).

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Correspondence to Zhenliang Sun.

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Sun, X., Wang, M., Liu, B. et al. Purification and characterization of angiotensin I converting enzyme inhibition peptides from sandworm Sipunculus nudus . J. Ocean Univ. China 16, 911–915 (2017). https://doi.org/10.1007/s11802-017-3293-9

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  • DOI: https://doi.org/10.1007/s11802-017-3293-9

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