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.
Similar content being viewed by others
References
Bougatef, A., Nedjar-Arroume, N., Ravallec-Plé, R., Leroy, Y., Guillochon, D., Barkia, A., and Nasri, M., 2008. Angiotensin I-converting enzyme (ACE) inhibitory activities of sardinelle (Sardinella aurita) by-products protein hydrolysates obtained by treatment with microbial and visceral fish serine proteases. Food Chemistry, 111: 350–356.
Byun, H. G., and Kim, S. K., 2001. Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin. Process Biochemistry, 36: 1155–1162.
Chen, J., Okada, T., Muramoto, K., Suetsuna, K., and Yang, S., 2003. Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein. Journal of Food Biochemistry, 26: 543–554.
Clemente, A., 2000. Enzymatic protein hydrolysates in human nutrition. Trends in Food Science & Technology, 11: 254–262.
Hartmann, R., and Meisel, H., 2007. Food-derived peptides with biological activity: From research to food applications. Current Opinion in Biotechnology, 18: 163–169.
He, H. L., Chen, X. L., Sun, C. Y., Zhang, Y. Z., and Zhou, B. C., 2006. Analysis of novel angiotensin I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis. Journal of Peptide Science, 12: 726–733.
Hernández-Álvarez, A. J., Carrasco-Castilla, J., Dávila-Ortiz, G., Alaiz, M., Girón-Calle, J., Vioque-Peña, J., Jacinto-Hernández, C., and Jiménez-Martínez, C., 2013. Angiotensin-converting enzyme-inhibitory activity in protein hydrolysates from normal and anthracnose disease-damaged Phaseolus vulgaris seeds. Journal of the Science of Food and Agriculture, 93: 961–966.
Li, G. H., Le, G. W., Shi, Y. H., and Shrestha, S., 2004. Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiology and pharmacological effects. Nutrition Research, 24: 469–486.
Liu, T., Wu, H., Zhao, C. Y., Xie, J., and Lin, Y., 2012. Analyse of Sipunculus nudus’s composition and study of its craft of enzymolysis. Food Industry, 33: 71–74.
Liu, X., Zhang, M., Jia, A., Zhang, Y., Zhu, H., Zhang, C., Sun, Z., and Liu, C., 2013. Purification and characterization of angiotensin I converting enzyme inhibitory peptides from jellyfish Rhopilema esculentum. Food Research International 50: 339–343.
Liu, X., Zhang, M., Shi, Y., Qiao, R., Tang, W., and Sun, Z., 2016. Produciton of the angiotensin I converting enzyme inhibitory peptides and isolation of four novel peptides from jellyfish (Rhopilema esculentum) protein hydrolysate. Journal of the Science of Food and Agirculture, 96: 3240–3248.
Matsui, T., Li, C. H., and Osajima, Y., 1999. Preparation and characterization of novel bioactive peptides responsible for angiotensin I-converting enzyme inhibition from wheat germ. Journal of Peptides Sciences, 5: 289–297.
Ondetti, M. A., Rubin, B., and Cushman, D. W., 1977. Design of specific inhibitor of angitotensin-converting enzyme–New class of orally active antihypertensive agents. Science, 196: 441–444.
Su, J., Jiang, L., Wu, J., Liu, Z., and Wu, Y., 2016. Anti-tumor and anti-virus activity of polysaccharides extracted from Sipunculus nudus (SNP) on Hepg2.2.15. International Journal of Biological Macromolecules, 87: 597–602.
Sun, X., Yang, J., Xu, Y., Liu, H., and Ren, Y., 2015. Study on hydrolysis conditions of Sipunculus nudus by response methodology. Food & Machinery, 31: 238–242.
Wijesekara, I., and Kim, S. K., 2010. Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: Prospects in the pharmaceutical industry. Marine Drugs, 8: 1080–1093.
Wu, H., He, H. L., Chen, X. L., Sun, C. Y., Zhang, Y. Z., and Zhou, B. C., 2008. Purification and identification of novel angiotensin-I-converting enzyme inhibitory peptides from shark meat hydrolysate. Process Biochemistry, 43: 457–461.
Zhang, C. X., and Dai, Z. R., 2011. Anti-hypoxia activity of a polysaccharide extracted from the Sipunculus nudus L. International Journal of Biological Macromolecules, 49: 523–526.
Zhang, C. X., Dai, Z. R., and Cai, Q. X., 2011. Anti-inflammatory and anti-nociceptive activities of Sipunculus nudus L. extract. Journal of Ethnopharmacology, 137: 1177–1182.
Zhao, Y., Li, B., Liu, Z., Dong, S., Zhao, X., and Zeng, M., 2007. Antihypertensive effect and purification of an ACE inhibition peptide from sea cucumber gelatin hydrolysate. Process Biochemistry, 42: 1586–1591.
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).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
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
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11802-017-3293-9