Antihypertensive Effect of Angiotensin I Converting Enzyme-Inhibitory Peptide from Hydrolysates of Bigeye Tuna Dark Muscle, Thunnus obesus

Angiotensin I converting enzyme (ACE) inhibitory peptide was isolated from tuna dark muscle hydrolysate prepared by alcalase, neutrase, pepsin, papain, α-chymotrypsin, and trypsin, respectively. Among hydrolysates, the pepsin-derived hydrolysate exhibited the highest ACE I inhibitory activity versus...

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Veröffentlicht in:	Journal of agricultural and food chemistry 2007-10, Vol.55 (21), p.8398-8403
Hauptverfasser:	Qian, Zhong-Ji, Je, Jae-Young, Kim, Se-Kwon
Format:	Artikel
Sprache:	eng
Schlagworte:	ACE inhibitory peptide Amino Acid Sequence angiotensin I converting enzyme inhbitors Angiotensin-Converting Enzyme Inhibitors - isolation & purification Angiotensin-Converting Enzyme Inhibitors - pharmacology Animals Antihypertensive Agents - pharmacology antihypertensive effect bioactive constituent Biological and medical sciences dark muscle enzyme inhibitors Food industries Fundamental and applied biological sciences. Psychology Hydrolysis hypertension kinetics Male Muscle Proteins - chemistry Muscle Proteins - isolation & purification Muscles - chemistry oral administration Peptide Hydrolases - metabolism peptides Peptides - chemistry Peptides - isolation & purification Peptides - pharmacology protein hydrolysates Rats Rats, Inbred SHR skeletal muscle Thunnus obesus Tuna tuna dark muscle
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