Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate

@inproceedings{Paiva2016IsolationAC,
  title={Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate},
  author={Lisete Sousa Paiva and Elisabete M C Lima and Ana Isabel Afonso Neto and Jos{\'e} Antonio Avelar Baptista},
  year={2016}
}
Abstract Ulva rigida protein was hydrolysed with pepsin plus bromelain after a screening of nine enzymes for optimal proteolysis. This hydrolysate, presenting ACE-inhibitory activity with an IC 50 value of 0.483 mg/mL, was fractionated by ultrafiltration membranes into three molecular weight ranges ( 3 kDa). The 50 : 0.095 mg/mL) was purified using size-exclusion chromatography and reversed-phase high-performance liquid chromatography, yielding two active ACE-inhibitory purified peptides. Edman… CONTINUE READING

Similar Papers

Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-9 OF 9 CITATIONS