• Journal of Microbiology and Biotechnology
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• v.12 no.1
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• pp.59-64
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• 2002

An angiotensin I-converting enzyme (EC 3.4.15.1) (ACE), which can convert inactive angiotensin I into angiotensin II, a vasoconstrictor, is one of the key enzymes in controlling hypertension. It is suggested that the inhibition of ACE prevents hypertension, and many inhibitory peptides have already been reported. In the current study, oligonucleotides encoding ACE inhibitory peptides (IY, VKY) were chemically synthesized and designed to be multimerised due to isoschizomer sites (BamHI, BglII). The cloned gene named AP3 was multimerised up to 6 times in pBluescript and expressed in BL2l containing pGEX-KG. The fusion protein (GST-AP3) was easily purified with a high recovery by an affinity resin, yielding 38 mg of synthetic AP3 from a 1-1 culture. The digestion of AP3 by chymotrypsin exhibited an $IC_50$ value of $18.53{\mu}M$. In conclusion, the present experiment indicated that AP3 could be used as a dietary antihypertensive drug, since the potent ACE inhibitory activity of AP3 could be activated by chymotrypsin in human intestine.

• 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.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.34 no.2
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• pp.164-172
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• 2001

The angiotensin-I converting enzyme (ACE) inhibitors from laver hydrolysate was isolated. Among the 13 kinds of proteases, Maxazyme NNP was most effective for preparing the high ACE inhibitory compound. In extraction conditions of ACE inhibitory peptide from laver hydrolysate, ACE inhibitory activity of hydrolysate treated with diethylether for decolorization and that of $70\%$ ethanol soluble fraction among the different ethanol concentrations were higher than other preparations. Low molecular fraction less than 3,000 dalton of layer hydrolysate separated by ultrafiltration had the highest ACE inhibitory activity, for further separation of ACE inhibitory peptide from laver hydrolysate, gel filtration chromatography (Sephadex G-25), reverse-phase HPLC (ODS & Vydac C-18) and gel permeation chromatography (Superdex Peptide HR) were performed. The molecular mass of the ACE inhibitory peptide fractions of gel permeation chromatography determined by electrospray-mass spectrometer were 413.48 (S1O2V2V1P),346.86 (S1O2V2V2P) and 320.32 (S2O6V3V1P) dalton and their amino acid sequence were Val-Gln-Gly-Asn, Thr-Glu-Thr and Phe-Arg, respectively.

• YAKHAK HOEJI
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• v.45 no.1
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• pp.93-100
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• 2001

Drug inetraction between of enalapril-induced angiotensin converting enzym) inhibitory effect and Ginkgo biloba Ext.-induced antioxidant action was evaluated in spontaneously hypertensive rats. Combination treatment of enalapril (20 mg/kg/day p.o.) and Ginkgo biloba Ext. (60 mg/kg/day, p.o.) for 6 weeks in drinking water to SHRs resulted the inhibition of ACE activity in lung tissue, angiotensin I-induced pressure response and plasma angiotensin II concentration as similar to enalapril alone treatment. But these effects were sustained after 1 week withdrawal of enalapril and Ginkgo biloba Ext. co-administeration. Also, coadministered group did not increase the concentration of bradykinin in lung tissue, which were different from enalapril alone treated group. Co-administration of enalapril and Ginkgo biloba Ext. inhibited the hemolysis induced by UV B type, even Ginkgo biloba Ext. alone treated group did not. These results suggested that Ginkgo biloba Ext. sustained ACE inhibitory effect and reduced the inhibitory effect of bradykinin inactivation induced by enalapril, meanwhile, enalapril increased the antioxidant effect of Ginkgo biloba Ext.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.9
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• pp.1384-1389
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• 2003

In order to clarify one of the biological functions of pork, we investigated whether a peptic hydrolysate of denatured porcine crude myosin showed inhibitory activity against angiotensin I-converting enzyme (ACE), which contributed to hypertension. Our results indicated that this hydrolysate showed relatively strong activity, and we therefore attempted to separate the involved peptides, which were considered to be active substances. To isolate these active peptides, the hydrolysate was separated using a solidphase separation, gel filtration high-performance liquid chromatography (HPLC), and two kinds of reverse phase HPLC. In each stage of separation, many fractions were detected, almost all of which showed ACE inhibitory activity. Thus, we suggested that the activity of the hydrolysate as a whole was a result of the activities of the many individual peptides. Six peaks were distinguished, with yields from 34 to 596 ppm of original crude myosin. In addition to the six peaks, many other active fractions were found throughout the separation steps, strongly suggesting that whole porcine crude myosin itself had ACE inhibitory activity. Moreover, pork as food was considered to function as an ACE inhibitory material in vivo, because pork proteins consist primarily of crude myosin, which included almost all the myofibrillar structural proteins.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.4
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• pp.427-431
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• 1999

This study was conducted to investigate the inhibitory activity of water extracts and its enzymatic hydrolysates from algae against angiotensin-I converting enzyme (ACE). The 7 kinds of algae were extracted with water at $50^{\circ}C,\;70^{\circ}C$ and $98^{\circ}C$. ACE inhibitory activities of water extracts were the highest at $70^{\circ}C$, and those of ceylon moss, layer, green layer, sea mustard, seaweed fusiforme sea tangle and sea staghorn were $10.9\%,\;9.3\%,\;8.9\%,\;8.2\%,\;7.5\%,\;7.1\%$ and $7.0\%$, respectively. Layer, green laver sea mustard and ceylon moss of high ACE inhibitory activities among the 7 kinds of water extracts were hydrolyzed by maxazyme and papain during 24hrs. ACE inhibitory activity of enzymatic hydrolysates was higher than that of water extracts, and was the highest in enzymatic hydrolysates of laver among the tested samples. In laver hydrolysates by proteases, the highest ACE inhibitory activity and peptide-nitrogen contents were observed at 8 hours hydrolysis and the hydrolysates by maxazyme showed relatively higher activity than those by papain(31.3 and $27.9\%$, respectively). But peptide-nitrogen contents were greater in papain hydrolysates than in maxazyme.

• Korean Journal of Food Science and Technology
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• v.29 no.6
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• pp.1316-1318
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• 1997

The isolated ${\kappa}-Casein$ on gel permeation chromatography was hydrolyzed by chymosin, trypsin, and pepsin. The 3% TCA soluble portion of the hydrolysates were dialyzed on the angiotensin-I converting enzyme (ACE) inhibition rate (%,) and inhibitory activity $(IC_{50})$ were determined. The trypsin hydrolysate exhibited the highest ACE inhibition rate while the chymosin hydrolysation showed the lowest activity. The hydrolysate was dialyzed using dialysis membrane with various molecular cut-offs, and $IC_{50}$ was determined. As the pore size of the dialysis tubing increased, the ACE inhibitory activity decreased.

• Journal of Dairy Science and Biotechnology
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• v.32 no.1
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• pp.7-16
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• 2014

Angiotensin-I-converting enzyme (ACE) inhibitory peptides have functional and potential properties of casein hydrolysates that are used in the development of food ingredients and anti-hypertensive hydrolysates derived from sodium caseinate enzymatic hydrolysates. Sodium caseinate could be treated by various kinds of commercial proteases, and then could be treated with the enzyme combination. Ultrafiltration treatment can be used to generate hydrolysates that can be used to determine ACE inhibitory activity. In general, hydrolysate quality can be evaluated by changes in hydrolysis characteristics, ACE inhibitory activity, as well as functional properties such as solubility, foam capacity, cytotoxicity, free radical-scavenging effects, and sensory evaluation. In this review, we present an overview of the ACE inhibitory peptides obtained by performing enzymatic hydrolysis on various sources to identify food ingredients and functional foods that reduce hypertension.

• Food Science of Animal Resources
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• v.31 no.5
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• pp.663-667
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• 2011

This study was performed to measure the angiotensin I-converting enzyme (ACE) inhibitory activity of peptide extracts derived from the enzymatic proteolysis of Hanwoo Musculus longissimus (M. longissimus) during cold storage. Thermolysin (80 ppm, w/w) and protease type XIII (100 ppm, w/w) were injected separately or in combination for the enzymatic proteolysis of sarcoplasmic and myofibrillar proteins prior to storage at $5^{\circ}C$ (T1) or at $-1^{\circ}C$ (T2) in a chilling room for 9 days. Beef injected with thermolysin (E2) and thermolysin+protease type XIII (E3) showed a significantly higher degree of hydrolysis at both storage temperatures (p<0.05). During the storage period, T1E2 at day 6 and T1E3 at day 9 showed the strongest ACE inhibitory activity with sarcoplasmic and myofibrillar protein proteolysates. Macromolecules greater than 10,000 Da were removed by ultra filtration, and the filtrates were separated into fractions using gel filtration. Five and three major fractions were collected from S-T1E2-6 and M-T1E3-9 extracts, respectively, and the $4^{th}$ fraction of the S-T1E2-6 extracts showed the highest ACE inhibitory rate of $61.96{\pm}7.41%$.

• Journal of Microbiology and Biotechnology
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• v.25 no.8
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• pp.1315-1320
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• 2015

To enhance the γ-aminobutyric acid (GABA) content, the optimized fermentation of soybean with added sea tangle extract was evaluated at 30℃ and pH 5.0. The medium was first inoculated with Aspergillus oryzae strain FMB S46471 and fermented for 3 days, followed by the subsequent inoculation with Lactobacillus brevis GABA 100. After fermentation for 7 days, the fermented soybean showed approximately 1.9 g/kg GABA and exhibited higher ACE inhibitory activity than the traditional soybean product. Furthermore, several peptides in the fraction containing the highest ACE inhibitory activity were identified. The novel fermented soybean enriched with GABA and ACE inhibitory components has great pharmaceutical and functional food values.