Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates derived from sardine muscle.
Hydrolyzates which inhibit the angiotensin I-converting enzyme (ACE) were prepared from sardine muscle by Bacillus licheniformis alkaline protease. Considering the practical application of preparations as a functional food material, the best proteolytic conditions with respect to taste, solubility and ACE inhibitory activity were a 0.3 wt% addition of the enzyme and 17-h proteolysis at 50 degrees C and pH 9.0. The preparations under these conditions had potent activity (IC50 = 0.26 mg protein/ml). Fractionation of the preparations on an ODS column with ethanol resulted in the production of more potent inhibitors. The most potent activity was obtained when eluting with 10% ethanol (IC50 = 0.015 mg protein/ml). This fraction was apparently rich in acidic amino acids, poor in hydrophobic ones, and effective for use as a physiologically functional food material by virtue of little bitterness, a fish odor and powerful ACE inhibitory activity.
Matsui
T
T
Department of Food Science and Technology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Matsufuji
H
H
Seki
E
E
Osajima
K
K
Nakashima
M
M
Osajima
Y
Y
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000378:metabolism*; D000818:Animals; D001407:Bacillus / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism*; D005399:Fishes; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009132:Muscles / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet
D000596:Amino Acids; D000806:Angiotensin-Converting Enzyme Inhibitors; D010450:Endopeptidases