• Korean Journal of Food Science and Technology
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• v.31 no.3
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• pp.848-854
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• 1999

Inhibitory compounds of angiotensin converting enzyme (ACE) were separated from Doenjang (traditional Korean fermented soybean paste). Water extracts from Doenjang which showed ACE inhibitory activity were separated with gel permeation chromatography (GPC), in which two fractions with high ACE inhibitory activities were obtained. The first fraction from GPC was further isolated by semi-preparative reverse phase preparative-HPLC (high performance liquid chromatography) and 2-dimensional electrophoresis/thin layer chromatography (TLC). The purified spot had molecular weight of 759 daltons and ninhydrin-positive non-peptide. The second fraction from GPC was also further isolated by semi-preparative reverse phase HPLC and $NH_2-column$ HPLC. One fraction with high ACE inhibitory activity was purified and characterized. Molecular weight of this fraction by LC-MS was 272.34 daltons. The active fraction was identified as Arg-Pro with ACE $IC_{50}$ of $92\;{\mu}M$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.4
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• pp.594-599
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• 2001

This study was attempted to isolate and identify the strain revealing high angiotensin converting enzyme (ACE) inhibitory activity from various soy fermented foods, i.e. meju, soybean paste and soy sauce. Forty-two strains with morphologically different characteristics were selected and the ACE inhibitory and proteolytic activities were examined. Of the strains tested, SS103 which was isolated from soy sauce showed the highest ACE inhibitory and proteolytic activities and was finally selected for further studies. The SS103 strain showed motility, rod form and ellipsoidal spores. The shape of colonies on the agar media was irregular, mucoidal and surface dull. The strain could grow under aerobic conditions of pH 5~9 and 10~$50^{\circ}C$. Main cellular fatty acid was $C_{15:0}$ anteiso, $C_{17:0}$ cis and $C_{17:0}$ iso, which was 33.9%, 18.8% and 16.5%, respectively. Based upon these morphological, biochemical and cultural properties, SS103 was identified as a Bacillus subtilis. Optimum cultural condition of Bacillus subtilis SS103 was pH 8.0, $37^{\circ}C$ and 48 hr.48 hr.

• Fisheries and Aquatic Sciences
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• v.19 no.7
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• pp.29.1-29.6
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• 2016

In the present study, we investigated to the antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities of the northern shrimp (Pandalus borealis) by-products (PBB) hydrolysates prepared by enzymatic hydrolysis. The antioxidant and ACE inhibitory activities of five enzymatic hydrolysates (alcalase, protamex, flavourzyme, papain, and trypsin) of PBB were evaluated by the 2, 2'-azino-bis [3-ethylbenzothiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities, reducing power and Li's method for ACE inhibitory activity. Of these PBB hydrolysates, the protamex hydrolysate exhibited the most potent ACE inhibitory activity with $IC_{50}$ value of $0.08{\pm}0.00mg/mL$. The PBB protamex hydrolysate was fractionated by two ultrafiltration membranes with 3 and 10 kDa (below 3 kDa, between 3 and 10 kDa, and above 10 kDa). These three fractions were evaluated for the total amino acids composition, antioxidant, and ACE inhibitory activities. Among these fractions, the < 3 kDa and 3-10 kDa fractions showed more potent $ABTS^+$ radical scavenging activity than that of > 10 kDa fraction, while the > 10 kDa fraction exhibited the significant reducing power than others. In addition, 3-10 kDa and > 10 kDa fractions showed the significant ACE inhibitory activity. These results suggested that the high molecular weight enzymatic hydrolysate derived from PBB could be used for control oxidative stress and prevent hypertension.

• Fisheries and Aquatic Sciences
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• v.8 no.2
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• pp.109-112
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• 2005

A peptide that inhibits angiotensin-converting enzyme (ACE) was isolated from a hydrolysate of Manila clam (Ruditapes philippinarum) proteins prepared with thermolysin. Amino acid sequence of the peptide was determined to be Leu-Leu-Pro. Chemically synthesized Leu-Leu-Pro had an $IC_{50}\;value\;of\;158\;\mu{M}$. Peptides related to the Manila clam-derived peptide were synthesized to study the structure-activity relationships. The tetrapeptide, Leu-Leu-Pro-Pro, had a very weak effect on the enzyme. However, Leu-Leu-Pro-Asn showed no inhibitory activity.

• Korean Journal of Food Science and Technology
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• v.25 no.5
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• pp.456-460
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• 1993

The present study was conducted to investigate Angiotensin I-converting enzyme(ACE) inhibition activity of the components of traditional tea materials in Korea. Angiotensin I-converting enzyme(ACE) inhibition activity of water soluble fractions obtained from the samples were strong in Zingiberis rhizoma, Acantopanacis cortex, Schizandrae fructus, Perilla semen, Cassiae torae semen, Zizyphy fructus in order. ACE inhibition activity of fractions obtained from methanol extract of Cassiae torae semen were strong in ethyl acetate fraction, ethyl ether fraction, water fraction, chloroform fraction in order. Compound C showed the strongest ACE inhibition activity among compound A, B, C, D separated from Cassiae torae semen, but Compound C separated from Cassiae torae semen was lower than bradykinin in the ACE inhibition activity.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1318-1323
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• 2004

This study describes the purification and characterization of a novel antihypertensive angiotensin 1­converting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at $30^{\circ}C$ and its ACE inhibitory activity was increased by about 1.5 times after treatment of the cell-free extract with pepsin. After the purification of ACE inhibitory peptides with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.07 mg and $3.5\%$ yield was obtained. The purified peptide was a novel decapeptide, showing very low similarity to other ACE inhibitory peptide sequences, and its amino acid sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor competitively inhibited ACE and also showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg body weight.

• Preventive Nutrition and Food Science
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• v.20 no.3
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• pp.176-182
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• 2015

Abalone protein was hydrolyzed by enzymatic hydrolysis and the optimal enzyme/substrate (E/S) ratios were determined. Abalone protein hydrolysates (APH) produced by Protamex at E/S ratio of 1:100 showed angiotensin I converting enzyme inhibitory activity with $IC_{50}$ of 0.46 mg/mL, and APH obtained by Flavourzyme at E/S ratio of 1:100 possessed the oxygen radical absorbance capacity value of $457.6{\mu}M$ trolox equivalent/mg sample. Flavourzyme abalone protein hydrolysates (FAPH) also exhibited $H_2O_2$ scavenging activity with $IC_{50}$ of 0.48 mg/mL and $Fe^{2+}$+ chelating activity with $IC_{50}$ of 2.26 mg/mL as well as high reducing power. FAPH significantly (P<0.05) protected $H_2O_2$-induced hepatic cell damage in cultured hepatocytes, and the cell viability was restored to 90.27% in the presence of FAPH. FAPH exhibited 46.20% intracellular ROS scavenging activity and 57.89% lipid peroxidation inhibition activity in cultured hepatocytes. Overall, APH may be useful as an ingredient for functional foods.

• Preventive Nutrition and Food Science
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• v.5 no.2
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• pp.75-80
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• 2000

To separate ACE inhibitors from edible plants, spices, and herbs, 285 extracts of 95 sources were screened for ACE inhibitory activity. The extract of Sinapis alba L. had the most potent ACE inhibitory activity. Mustard seeds were crushed homogeneously and extracted with hexane and water successively. Lyophilized water extract was fractionated with $H_2O$:butanol(1:1). The ACE inhibitor was purified from butanol fraction by methanol precipi-tation, gel filtration, HPLC, and FPLC with Superdex peptide HQ 10/30 column. The active fraction has been purified to homogeneity, which was proven by gel filtration using FPLC system. The yield was 0.02%. The com-pound has a molecular weight of about 640. The compound competitively inhibited ACE activity and the $IC_{50}$ value was 79$\mu\textrm{g}$/ml. The purified compound showed uterus contraction activity in isolated rat uterus.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.26 no.4
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• pp.321-329
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• 1993

The present study was conducted to elucidate the body modulating function of fermented seafood products. Angiotensin converting enzyme (ACE) acts in blood pressure regulation, converting angiotensin I to the potent vasoconstrictor angiotensin II and inactivating the vasodilator bradykinin to raise blood pressure. Salted and fermented anchovy which is one of the traditional fermented seafood in Korea was tested for inhibitory activity against ACE. ACE inhibitory activity of salted anchovy during the period of fermentation was increased with the elapse of fermentation days until fermentation of 60 days, but thereafter decreased inversely. When the fermented product was extracted with $50\%$ ethanol, the ACE inhibitory activity was the highest. And the ACE inhibitory activity was proportion to the content of $50\%$ ethanol soluble peptide-nitrogen of the fermented product. From the profiles of gel permeation chromatography on a Bio-Gel P-2 of $50\%$ ethanol soluble fraction obtained from salted and fermented anchovy fermented for 60 days at an ambient temperature, the higher activity fractions were C'($IC_{50}=97{\mu}g\;protein/ml$) and D'($IC_{50}=65{\mu}g\;protein/ml$). Amino acid analysis showed that the large quantify of threonine, glutamic acid, lysine for C' and serine, proline for D', respectively.

• Biomolecules & Therapeutics
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• v.1 no.2
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• pp.220-225
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• 1993

Effect of BR-900317 on the angiotensin I-induced pressor response in pithed rats and the effects of its single oral administration on plasma angiotensin converting enzyme (ACE) activities in normotensive rats and on the cardiovascular system in hypertensive model rats (SHR, RHR), were compared with those of captopril. BR-900317 attenuated the angiotensin I-induced pressor effects in pithed rats. In a single oral dose administration study, BR-900317 inhibited the plasma ACE activities in a dose-dependent fashion. Duration of the action of BR-900317 was similar to that of captopril. BR-900317 produced antihypertensive effect in spontaneously hypertensive rats and dose-dependent antihypertensive effect in 2-kidney Goldblatt hypertensive rats without affecting heart rate. These results suggest that the main mechanism of the antihypertensive effect of BR-900317 is the suppression of angiotensin II production due to the inhibition of the ACE.