Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.

@article{Saiga2008AngiotensinIE,
  title={Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate.},
  author={Ai Saiga and Koji Iwai and Toru Hayakawa and Yoshihisa Takahata and Shiniich Kitamura and Toshihide Nishimura and Fumiki Morimatsu},
  journal={Journal of agricultural and food chemistry},
  year={2008},
  volume={56 20},
  pages={9586-91}
}
In this study, collagen extracted from chicken legs (which are the yellow keratin parts containing a nail) was hydrolyzed with various enzymes, and the angiotensin I-converting enzyme (ACE)-inhibitory activity of each hydrolysate was determined. The hydrolysate by treatment with an Aspergillus species-derived enzyme had the highest activity (IC 50 = 260 microg/mL). The fraction of this hydrolysate obtained by ultrafiltration with a molecular-weight cutoff of 3000 Da (low fraction) had a… CONTINUE READING

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