Skip to main content
Log in

Angiotensin I-Converting Enzyme Inhibitory Proteins and Peptides from the Rhizomes of Zingiberaceae Plants

  • Published:
Applied Biochemistry and Biotechnology Aims and scope Submit manuscript

Abstract

Ammonium sulphate cut protein extracts, and their pepsin hydrolysates, from the rhizomes of 15 plants in the Zingiberaceae family were screened for their in vitro angiotensin I-converting enzyme inhibitory (ACEI) activity. The protein extract from Zingiber ottensii had the highest ACEI activity (IC50 of 7.30 × 10−7 mg protein/mL) and was enriched for by SP Sepharose chromatography with five NaCl step gradients 0, 0.25, 0.50, 0.75 and 1 M NaCl collecting the corresponding five fractions. The highest ACEI activity was found in the F75 fraction, which appeared to contain a single 20.7-kDa protein, suggesting enrichment to or near to homogeneity. The ACEI activity of the F75 fraction was moderately thermostable (−20–60 °C), showed >80% activity across a broad pH range of 4–12 (optimal at pH 4–5) and appeared as a competitive inhibitor of ACE (K i of 9.1 × 10−5 mg protein/mL). For the pepsin hydrolysates, that from Zingiber cassumunar revealed the highest ACEI activity (IC50 of 0.38 ± 0.012 mg/mL), was enriched to a single active hexapeptide by RP-HPLC with a strong ACEI activity (IC50 of 0.011 ± 0.012 mg/mL) and acted as a competitive inhibitor of ACE (K i of 1.25 × 10−6 mg protein/mL).

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6

Similar content being viewed by others

References

  1. Guyton, A. C., & Hall, J. E. (2006). Textbook of medical physiology (11th ed.). Philadelphia: Elsevier Saunders.

    Google Scholar 

  2. Egan, B. M., Basile, J. N., & Lackland, D. T. (2004). Hypertension: Hot topics. Philadelphia: Hanley & Belfus, Inc.

    Google Scholar 

  3. Ganten, D., Unger, T., & Lang, R. E. (1984). Arzneimittel-Forschung, 34, 1391–1398.

    CAS  Google Scholar 

  4. Kostis, J. B., & DeFelice, E. A. (1987). Angiotensin converting enzyme inhibitors. New York: Alan R. Liss., Inc.

    Google Scholar 

  5. Brown, N. J., & Vaughan, D. E. (1998). Circulation, 97, 1411–1420.

    CAS  Google Scholar 

  6. Pihlanto, A., & Korhonen, H. (2003). Advances in Food and Nutrition Research, 47, 175–276.

    Article  CAS  Google Scholar 

  7. Kitts, D. D., & Weiler, K. (2003). Current Pharmaceutical Design, 9, 1309–1323.

    Article  CAS  Google Scholar 

  8. Möller, N. P., Scholz-Ahrens, K. E., Roos, N., & Schrezenmeir, J. (2008). European Journal of Nutrition, 47, 171–182.

    Article  Google Scholar 

  9. Larsen, K. (1980). Natural History Bulletin of the Siam Society, 151–169.

  10. Je, J. Y., Park, P. J., Kim, E. K., & Ahn, C. B. (2009). Food Chemistry, 113, 932–935.

    Article  CAS  Google Scholar 

  11. Bradford, M. M. (1976). Analytical Biochemistry, 72, 248–254.

    Article  CAS  Google Scholar 

  12. Laemmli, U. K. (1970). Nature, 227, 680–685.

    Article  CAS  Google Scholar 

  13. Tiptara, P., Petsom, A., Roengsumran, S., & Sangvanich, P. (2008). Journal of the Science of Food and Agriculture, 88, 1025–1034.

    Article  CAS  Google Scholar 

  14. Mortz, E., Vorm, O., Mann, M., & Roepstorff, P. (1994). Biological Mass Spectrometry, 23, 249–261.

    Article  CAS  Google Scholar 

  15. Arihara, K., Nakashima, T., Mukai, T., Ishikawa, S., & Itoh, M. (2001). Meat Science, 57, 319–324.

    Article  CAS  Google Scholar 

  16. Demir, Y., Güngör, A. A., Duran, E. D., & Demir, N. (2008). Food Technology and Biotechnology, 46, 286–291.

    CAS  Google Scholar 

  17. Rameshwaram, N. R., & Nadimpalli, S. K. (2008). Journal of Chromatography B, 861, 209–217.

    Article  CAS  Google Scholar 

  18. Wang, S., Ng, T., Chen, T., Lin, D., Wu, J., Rao, P., et al. (2005). Biochemical and Biophysical Research Communications, 327, 820–827.

    Article  CAS  Google Scholar 

  19. Ye, X. Y., & Ng, T. B. (2001). Journal of Protein Chemistry, 20, 353–359.

    Article  CAS  Google Scholar 

  20. Tiengburanatam, N., Boonmee, A., Sangvanich, P., & Karnchanatat, A. (2010). Applied Biochemistry and Biotechnology, 162, 1938–1951.

    Article  CAS  Google Scholar 

  21. Emmermann, M., Clericus, M., Braun, H. P., Mozo, T., Heins, L., Kruft, V., et al. (1994). Plant Molecular Biology, 25, 271–281.

    Article  CAS  Google Scholar 

  22. Mallikarjun, G. K. G., Gowda, L. R., Rao, A. G., & Prakash, V. (2006). Journal of Agricultural and Food Chemistry, 54, 4568–4573.

    Article  Google Scholar 

Download references

Acknowledgments

The authors thank the 90th Anniversary of Chulalongkorn University fund, the National Research University Project of CHE, the Ratchadaphiseksomphot Endowment Fund (AG001B, AM1019A and AS613A), the Thai Government Stimulus Package 2 (TKK2555) and the Thailand Research Fund through the TRF-CHE Research Grant for Mid-Career University Faculty (RMU5380036), for financial support of this research, as well as the Institute of Biotechnology and Genetic Engineering for support and facilities. We also thank Dr. Robert Butcher (Publication Counseling Unit, Chulalongkorn University) for his constructive comments in preparing this manuscript.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Polkit Sangvanich.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Yodjun, M., Karnchanatat, A. & Sangvanich, P. Angiotensin I-Converting Enzyme Inhibitory Proteins and Peptides from the Rhizomes of Zingiberaceae Plants. Appl Biochem Biotechnol 166, 2037–2050 (2012). https://doi.org/10.1007/s12010-012-9630-y

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12010-012-9630-y

Keywords

Navigation