Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Elk (Cervus elaphus) Velvet Antler

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Elk (Cervus elaphus) Velvet Antler

Angiotensin I-converting enzyme (ACE) inhibitory activities of elk antler hydrolysates prepared with three kinds of proteases, pepsin, trypsin and α-chymotrypsin, were investigated. The ACE inhibitory activity of the pepsinolytic hydrolysate was the highest with an IC∧50 value of 9.3 ㎍/mL. In additi...

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Veröffentlicht in:Journal of food science and nutrition (Pusan, Korea : 2003) Korea : 2003), 2005-09, Vol.10 (3)
Hauptverfasser: Karawita, Rohan (Cheju National University, Jeju, Republic of Korea), Park, P.J. (Konkuk University, Chungju, Republic of Korea), Siriwardhana, Nalin (Cheju National University, Jeju, Republic of Korea), Jeon, B.T. (Konkuk University, Chungju, Republic of Korea), Moon, S.H. (Konkuk University, Chungju, Republic of Korea), Ahn, D.K. (Jaseng Research Institute of Bio-Technology and Bioscience, Seoul, Republic of Korea), Cho, S.K. (Cheju National University, Jeju, Republic of Korea), Jeon, Y.J. (Cheju National University, Jeju, Republic of Korea), E-mail: youjinj@cheju.ac.kr
Format: Artikel
Sprache:eng
Schlagworte:
ANDOUILLER
angiotensin I-converting enzyme (ACE)
ANTLERS
ASTAS
hydrolysate
PEPTIDE
PEPTIDES
PEPTIDOS
PROTEOLISIS
PROTEOLYSE
PROTEOLYSIS
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Zusammenfassung:Angiotensin I-converting enzyme (ACE) inhibitory activities of elk antler hydrolysates prepared with three kinds of proteases, pepsin, trypsin and α-chymotrypsin, were investigated. The ACE inhibitory activity of the pepsinolytic hydrolysate was the highest with an IC∧50 value of 9.3 ㎍/mL. In addition, three kinds of pepsinolytic hydrolysates with relatively high molecular weights (over 10,000 Da), medium molecular weights (5,000 to 10,000 Da), and low molecular weights (below 5,000 Da) were fractionated using an ultrafiltration membrane system. The below 5,000 Da hydrolysate exhibited the highest ACE inhibitory activity.
ISSN:1226-332X