Angiotensin I converting enzyme inhibitory peptides produced by autolysis reactions from wheat bran.
The production of angiotensin I converting enzyme (ACE) inhibitory peptides by autolysis reactions from wheat milling byproducts was investigated. Milled whole grain, bran, shorts, and red dog acquired ACE inhibitory activity though water soaking treatment. Among the milled fractions, the preparation of shorts exhibited the strongest inhibitory activity (IC50 = 0.08 mg protein/mL) followed by that of bran, red dog, and whole grain in decreasing order. The production of ACE inhibitory peptides was almost completely inhibited by pepstatin A, indicating the contribution of aspartic proteases. The optimal pH for acquiring ACE inhibitory activity of the byproduct fraction (mixtures of bran and shorts) was 3.2. The level of inhibitory activity rose with increasing temperature up to 40 degrees C. The inhibitory activity reached a maximal level after a 12 h reaction time and maintained the same level up to 24 h at 40 degrees C, pH 3.2. From the hydrolysate of the byproduct fraction, six peptides were isolated by several steps of chromatography, and their amino acid sequences were Leu-Gln-Pro, Ile-Gln-Pro, Leu-Arg-Pro, Val-Tyr, Ile-Tyr, and Thr-Phe. Thus, wheat milling byproducts have the possibility to become an effective source for ACE inhibitory peptides.
Nogata
Yoichi
Y
National Agricultural Research Center for Western Region, 6-12-1 Nishifukatsu, Fukuyama, Hiroshima 721-8514, Japan. ynogata@affrc.go.jp
Nagamine
Takashi
T
Yanaka
Mikiko
M
Ohta
Hideaki
H
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry*; D004043:Dietary Fiber / Q000032:analysis*; D005511:Food Handling / Q000379:methods*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D014908:Triticum / Q000737:chemistry*
D000806:Angiotensin-Converting Enzyme Inhibitors; D004043:Dietary Fiber; D010455:Peptides