Aim: The angiotensin-I-converting enzyme (ACE) inhibitory and antihypertensive activities of wakame hydrolysates have been investigated in several studies. Methods: Wakame (Undaria pinnatifida) was hydrolyzed using 17 kinds of proteases and the inhibitory activity of the hydrolysates for ACE was measured. Of these hydrolysates 4 with potent ACE inhibitory activity were administered singly and orally to spontaneously hypertensive rats (SHR). Results: The systolic blood pressure of SHR decreased significantly after single oral administration of protease S ‘Amano’ and proleather FG-F hydrolysates (10 mg protein/kg body weight). In a long-term feeding experiment, 7-week-old SHR were fed standard chow supplemented with protease S ‘Amano’-derived wakame hydrolysates for 10 weeks. In SHR fed the 1 and 0.1% wakame hydrolysates, elevation of systolic blood pressure was still significantly suppressed for 7 weeks. Conclusions: The hydrolysates derived from wakame by protease S ‘Amano’ have a powerful ACE-inhibitory activity (IC50 = 86 µg protein/ml) and were effective in spite of their slight bitterness as ‘physiologically functional food’ with antihypertensive activity.
The photon emission (chemiluminescence; CL) of catechin in the presence of active oxygen species (hydrogen peroxide, hydroxyl radical tert-butyl hydroperoxide and tert-butyl oxyl radical) and acetaldehyde was confirmed to occur non-enzymatically at room temperature in aqueous neutral conditions. The CL intensity [P] in the presence of active oxygen species (X), catalytic species (Y) and receptors (Z) is predicted by [P] = k [X] [Y] [Z]. The calculated photon constants (k) of 8 catechins and gallic acid were 8.23 x 10(6) M-2 s-1 counts ((-)-epigallocatechin), 2.78 x 10(8) ((-)-epigallocatechin gallate), 4.66 x 10(5) ((-)-gallocatechin gallate), 4.36 x 10(5) ((-)-gallocatechin), 2.70 x 10(5) ((-)-epicatechin), 6.44 x 10(4) ((-)-catechin), 585 x 10(4) ((-)-epicatechin gallate), 4.78 x 10(4) (gallic acid) and 3.54 x 10(4) ((-)-catechin gallate), respectively. The system of active oxygen species, catalytic species and receptors is proposed to be a scavenging mechanism for active oxygen species. In the presence of acetaldehyde, (-)-epigallocatechin (maximum k value among catechins tested) reacted with tert-BuOOH to form tert-BuOH as determined by HPLC analysis.
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