A novel angiotensin I-converting enzyme (ACE) inhibitory peptide from a marine Chlorella ellipsoidea and its antihypertensive effect in spontaneously hypertensive rats

@article{Ko2012ANA,
  title={A novel angiotensin I-converting enzyme (ACE) inhibitory peptide from a marine Chlorella ellipsoidea and its antihypertensive effect in spontaneously hypertensive rats},
  author={Seok-Chun Ko and Nalae Kang and Eun-A. Kim and Min-Cheol Kang and Seung-Hong Lee and Sung-Myung Kang and Joon-Baek Lee and Byong Tae Jeon and Se-Kwon Kim and Sun Joo Park and Pyo Jam Park and Won‐Kyo Jung and Daekyung Kim and You-Jin Jeon},
  journal={Process Biochemistry},
  year={2012},
  volume={47},
  pages={2005-2011}
}

Purification and the secondary structure of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the alcalase hydrolysate of seahorse protein

The novel ACE-inhibiting peptide (PAGPRGPA) was isolated from the seahorse for the first time and may be used as a favorable ingredient in nutraceuticals, medicines, and functional foods against antihypertensive and related diseases.

A heptameric peptide purified from Spirulina sp. gastrointestinal hydrolysate inhibits angiotensin I-converting enzyme- and angiotensin II-induced vascular dysfunction in human endothelial cells

Results indicated that this Spirulina sp.-derived peptide warrants further investigation as a potential pharmacological inhibitor of ACE and vascular dysfunction.

Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis

The results point out the possibility of obtaining bioactive peptides from chia proteins by means of a controlled protein hydrolysis using Alcalase-Flavourzyme sequentional system.

Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia ( Salvia hispanica ) Produced by Enzymatic Hydrolysis Maira

The results point out the possibility of obtaining bioactive peptides from chia proteins by means of a controlled protein hydrolysis using Alcalase-Flavourzyme sequentional system.

Purification and identification of novel angiotensin-I converting enzyme (ACE) inhibitory peptides from cultured marine microalgae (Nannochloropsis oculata) protein hydrolysate

Results suggest that the isolated peptides from cultured marine microalga, N. oculata protein sources may have potentiality to use commercially as ACE inhibitory agents in functional food industry.

Purification and Characterization of Angiotensin-I Converting Enzyme Inhibitory Peptides from Prickly Ash (Zanthoxylum bungeanum Maxim) Seed Protein Hydrolysates

Abstract Prickly ash (Zanthoxylum bungeanum Maxim) seed protein was hydrolyzed with papain to obtain hydrolysates with inhibitory activity against angiotensin-I converting enzyme (ACE). ACE
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Effect of angiotensin I-converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of Styela plicata

The results of this study suggest that peptides derived from S. plicata may be beneficial as anti-hypertension compounds in functional foods resource.