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Isolation of Peptides with Angiotensin I‐converting Enzyme Inhibitory Effect Derived from Hydrolysate of Upstream Chum Salmon Muscle
Author(s) -
Ono S.,
Hosokawa M.,
Miyashita K.,
Takahashi K.
Publication year - 2003
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2003.tb12300.x
Subject(s) - hydrolysate , chemistry , thermolysin , enzyme , inhibitory postsynaptic potential , biochemistry , angiotensin converting enzyme , renin–angiotensin system , hydrolysis , food science , endocrinology , blood pressure , biology , trypsin
In order to utilize upstream chum salmon as a component of nutraceutical food, their defatted muscle proteins were hydrolyzed with 5% thermolysin. The resulting hydrolysate showed high inhibitory activity against angiotensin I‐converting enzyme (inhibitory concentration 50 = 27.9 protein μg/mL) in vitro. A significant reduction of systolic blood pressure was observed when 500 and 2000 mg/kg of body weight were orally administered into spontaneously hypertensive rats. Angiotensin I‐converting enzyme inhibitory peptides contained in the hydrolysate were isolated with various chromatographs. These 6 active peptides were Trp residue‐containing dipeptides: Trp‐Ala, Val‐Trp, Trp‐Met, Met‐Trp, Ile‐Trp, and Leu‐Trp. The inhibitory concentration 50 values of these dipeptides ranged from 2.5 μM to 277.3 μM.