Angiotensin I Converting Enzyme Inhibitory Activities of Various Fermented Foods

Okamoto, Akiko; Hanagata, Hiroshi; Matsumoto, Emiko; Kawamura, Yukio; Koizumi, Yukimichi; Yanagida, Fujitoshi

doi:10.1271/bbb.59.1147

Cited by 140 publications

(70 citation statements)

References 3 publications

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“…The results have indicated that the processing technique s h a v e a n i m p a c t o n t h e A C E -i n h i b i t o r y activities of soy products. Different fermented soybean foods showed IC50 values of 0.51 mg/ml for tempeh, 1.77 mg/ml for tofuyo, 3.44 and 0.71-17.80 mg/ml for soy sauce, 5.35 and 1.27 mg/ml for miso paste, and 0.16, 0.19 and 0.27 mg/ml for natto [24,75,76]. Commercial Chinese style soy paste exhibited ACE-inhibitory activities with the lowest and the highest IC50 values of 0.012 and 3.241 mg/ml, respectively [77].…”

Section: Production Of Peptidesmentioning

confidence: 99%

Antihypertensive Properties of Plant Protein Derived Peptides

Pihlanto¹,

Mäkinen²

2013

Bioactive Food Peptides in Health and Disease

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Section: Production Of Peptidesmentioning

confidence: 99%

Antihypertensive Properties of Plant Protein Derived Peptides

Pihlanto¹,

Mäkinen²

2013

Bioactive Food Peptides in Health and Disease

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“…Li et al (2010) reported that the ACE inhibitory activities of extracts from Chinese commercial fermented soy paste were significantly correlated with their color. Okamoto et al (1995) showed that soy sauces with light color showed lower ACE inhibitory activity than those with dark color. Thus, the ACE inhibitory activities of food ingredients may be correlated with their color.…”

Section: Effects Of Heat Treatment On the Color Of Bovine Casein-derimentioning

confidence: 99%

Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein

Zhang

et al. 2014

J. Zhejiang Univ. Sci. B

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This study investigated the effect of heat treatment combined with acid and alkali on the angiotensin-Iconverting enzyme (ACE) inhibitory activity of peptides derived from bovine casein. The free amino group content, color, and cytotoxicity of the peptides were measured under different conditions. When heated at 100 °C in the pH range from 9.0 to 12.0, ACE inhibitory activity was reduced and the appearance of the peptides was significantly darkened. After thermal treatment in the presence of acid and alkali, the free amino group content of ACE inhibitory peptides decreased markedly. High temperature and prolonged heating also resulted in the loss of ACE inhibitory activity, the loss of free amino groups, and the darker coloration of bovine casein-derived peptides. However, ACE inhibitory peptides, within a concentration range of from 0.01 to 0.2 mg/ml, showed no cytotoxicity to Caco-2 and ECV-304 cell lines after heat treatment. This indicated that high temperature and alkaline heat treatment impaired the stability of bovine casein-derived ACE inhibitory peptides.

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“…This enzyme catalyzes the cleavage of the C-terminal dipeptide from inactive angiotensin I (DRVYIHPFHL) to become active angiotensin II (DRVYIHPF) (Skeggs et al, 1956), and inhibits the activity of the vasodilator bradykinin (Erdos, 1975). Consequently, this concerted action endows ACE with a crucial role in controlling blood pressure (Okamoto et al, 1995).…”

mentioning

confidence: 99%

Antihypertensive Effect of an Enzymatic Hydrolysate of Chicken Essence Residues.

Chen

Liu

Yang

et al. 2002

FSTR

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Enzymatic hydrolysates with antihypertensive activity were obtained from the leftover residues of a chicken essence factory. Among many proteases tested, Alcalase was found to be the best to produce high angiotensin I-converting enzyme (ACE) inhibitory activity in vitro. The in vivo experiment revealed that a 3% supplement of the Alcalase-treated hydrolysate of chicken essence residues added to the control diet fed to spontaneously hypertensive rat (SHR) lowered the systolic blood pressure (SBP) of the rats after 16 weeks of treatment and at 1 week post-treatment. Repression of ACE activity of the aorta was suggested to be the reason for the antihypertensive effect of the Alcalasetreated hydrolysate of chicken essence residues.

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Angiotensin I Converting Enzyme Inhibitory Activities of Various Fermented Foods

Cited by 140 publications

References 3 publications

Antihypertensive Properties of Plant Protein Derived Peptides

Antihypertensive Properties of Plant Protein Derived Peptides

Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein

Antihypertensive Effect of an Enzymatic Hydrolysate of Chicken Essence Residues.

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