Characterization of ACE Inhibitory Peptides from Mactra veneriformis Hydrolysate by Nano-Liquid Chromatography Electrospray Ionization Mass Spectrometry (Nano-LC-ESI-MS) and Molecular Docking

@inproceedings{Liu2014CharacterizationOA,
  title={Characterization of ACE Inhibitory Peptides from Mactra veneriformis Hydrolysate by Nano-Liquid Chromatography Electrospray Ionization Mass Spectrometry (Nano-LC-ESI-MS) and Molecular Docking},
  author={Rui Liu and Yunhan Zhu and Jiao Chen and Hao Wu and Lei Shi and Xinzhi Wang and Lingchong Wang},
  booktitle={Marine drugs},
  year={2014}
}
Food-derived bioactive compounds are gaining increasing significance in life sciences. In the present study, we identified angiotensin I-converting enzyme (ACE)-inhibitory peptides from Mactra veneriformis hydrolysate using a nano-LC-MS/MS method. Mactra veneriformis hydrolysate was first separated into four fractions (F1-F4) based on molecular weight by ultrafiltration. The fraction with molecular weight lower than 1 kDa (F1) showed the highest ACE inhibitory activity. F1 was then analyzed by… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 2 times over the past 90 days. VIEW TWEETS

References

Publications referenced by this paper.
Showing 1-10 of 30 references

Isolation of novel bioactive regions from bovine Achilles tendon collagen having angiotensin I-converting enzyme-inhibitory properties

  • P. Banerjeel, C. Shanthi
  • Process Biochem
  • 2012
1 Excerpt

Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate

  • D. D. Pan, J. X. Cao, H. Q. Guo, B. Zhao
  • Food Chem
  • 2012
1 Excerpt

Similar Papers

Loading similar papers…