• Food Science of Animal Resources
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• v.22 no.1
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• pp.87-93
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• 2002

Angiotensiri-I converting enzyme(ACE) catalyst the removal of the C-terminal dipeptide from the angiotensin-I to give the angiotensin-II, a potent peptide that causes constriction of regulation of blood pressure. Recently, ACE inhibitor peptides have been isolated from enzymatic digests of food protein. The aim of this study was to identify bovine casein hydrolysates with ACE inhibitory properties in different enzymatic hydrolysis conditions. The casein were hydrolyzed neutrase, alcalase, protamax, flavourzyme, premed 192, sumizyme MP, sumizyme LP and pescalase alone and with an enzyme combination. Premed 192 produced ACE inhibitory peptides most efficiently. In order to ACE inhibitory peptide produced enzymatic hydrolysis condition were premed 192 added to casein ratio of 1:100(w/w), and incubated at 47$\^{C}$ for 12hrs. Casein hydrolysate gave 50% inhibition(IC$\_$50/ value) of ACE activity at concentration with 248ug/ml(general method) and 265ug/ml(pretreatment method) respectively.

• Journal of Microbiology and Biotechnology
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• v.16 no.5
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• pp.757-763
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• 2006

Angiotensin I-converting enzyme (ACE) inhibitors have generally been very useful to remedy or prevent hypertension. This study describes the extraction and characterization of an ACE inhibitor from the fruiting body of Pholiota adiposa ASI 24012, which can be used as an antihypertensive drug. The maximal ACE inhibitory activity $(IC_{50};0.25mg)$ was obtained when the fruiting body of Pholiota adiposa ASI 24012 was extracted with distilled water at $30^{\circ}C$ for 12 h. After the purification of ACE inhibitor with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.044 mg was obtained. The purified ACE inhibitory peptide was a novel pentapeptide, showing very little similarity to other ACE inhibitory peptide sequences. The molecular mass of the purified ACE inhibitor was estimated to be 414 daltons with a sequence of Gly-Glu-Gly-Gly-Pro, and showed a clear antihypertensive effect on spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg.

• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.4
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• pp.737-742
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• 2000

As functionality investigation of a soybean fermentation food, a angiotensin converting enzyme inhibitory peptide was separated during natto fermentation by Bacillus natto and inhibitory effect was investigated. After incubation at each 2$0^{\circ}C$, 3$0^{\circ}C$, 4$0^{\circ}C$, 5$0^{\circ}C$, 6$0^{\circ}C$ for the 0~72 hr, protein content, protease activity and angiotensin converting enzyme inhibition were determined. The protein content and protease activity were increased and reached maximum at 60 hr fermentation with 4$0^{\circ}C$ and decreased after the 60 hr fermentation during natto fermentation. The optimum condition for angiotensin converting enzyme inhibitors was appeared at fermentation for 60 hr at 4$0^{\circ}C$. Crude extract of natto was partially purified by Amicon membrane YM-3 and Sephadex G-10, G-25 gel filtration, stepwise. The inhibitory rate was increased in a concentration dependent manner, espcially the most potent activity about 74.74% at 1.0 mg peptide content. The most prominent amino acid of the peptide from natto was alanine, followed by phenylalnine, histidine.

• Microbiology and Biotechnology Letters
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• v.36 no.4
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• pp.291-298
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• 2008

The cardiovascular angiotensin I-converting enzyme inhibitory activity, fibrinolytic activity and bbb-secretase inhibitory activity of four kinds of red wine were investigated during fermentation and post-fermentation. After 10 days of fermentation, the antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activities of all the red wines ranged from 38.6% to 58.8%. However, the ACE inhibitory activities increased with the prolongation of the post-fermentation period; moreover, in the Vitis hybrid red wine, the ACE inhibitory activity reached its highest value, 76.9%, after 120 days of post-fermentation. During the fermentation and post-fermentation of all the red wines, fibrinolytic activity was weak or not detected. After 10 days of fermentation, Vitis labrusca B red wine exhibited the greatest antidementia $\beta$-secretase inhibitory activity of 54.8%, though $\beta$-secretase inhibitory activity decreased significantly to less than 10% during 120 days of post-fermentation. In conclusion, we obtained a highly valuable Vitis hybrid red wine that was fermented for 10 days at $25^{\circ}C$ with Vitis hybrid and S. cerevisiae K-7 and then post-fermentation for 120 days at $4^{\circ}C$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.38 no.2
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• pp.177-181
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• 2009

The peptides from Aroase AP10 enzymatic hydrolysates of octopus proteins were isolated and tested for inhibitory activity against angiotensin converting enzyme (ACE). The Aroase AP10 hydrolysates were filtered through PM-10 membrane (M.W. cut-off 10,000) to obtain the peptides fractions with ACE inhibition activity. These fractions were applied to a Biogel P-2 column. Three active fractions (A, B, and C) were collected and applied to a SuperQ-Toyopearl 650S column chromatography, leading to the isolation of four active fractions (A-1, A-2, B-1, and C-1). Among the active fractions, C-1 had the highest ACE inhibitory activity ($IC_{50}=3.10{\mu}g$). The main composition of its amino acids is arginine, lysine, histidine and leucine, which cover about 60% of the total amino acids.

• BMB Reports
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• v.35 no.2
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• pp.239-243
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• 2002

Angiotensin I that converts the enzyme (ACE) inhibitory peptide, Gly-Pro-Leu, previously purified and identified from the Alaskan pollack skin gelatin hydrolysate, were synthesized. In addition, the peptides Gly-Leu-Pro, Leu-Gly-Pro, Leu-Pro-Gly, Pro-Gly-Leu, Pro-Leu-Gly, Gly-Pro, and Pro-Leu, which consisted of glycine, proline, and leucine, were synthesized by the solid-phase method. The $IC_{50}$ values of each tripeptide - namely Leu-Gly-Pro, Gly-Leu-Pro, Gly-Pro-Leu, Pro-Leu-Gly, Leu-Pro-Gly, and Pro-Gly-Leu - were 0.72, 1.62, 2.65, 4.74, 5.73, and $13.93{\mu}M$, respectively. The ACE inhibitory activity of these tripeptides was higher than that of dipeptides, such as Gly-Pro and Pro-Leu with $IC_{50}$ values of 252.6 and $337.3\;{\mu}M$, respectively. Among the tripeptides, Leu-Gly-Pro and Gly-Leu-Pro had higher inhibitory activity than Gly-Pro-Leu that was isolated from the Alaskan pollack skin gelatin hydrolysate. Among the different types of tripeptides that were examined, the highest ACE inhibitory activity was observed for Leu-Gly-Pro. It had the leucine residue at the N-terminal and proline residue at the C-terminal.

• 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.

• Food Science and Biotechnology
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• v.17 no.4
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• pp.873-877
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• 2008

Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.

• Korean Journal of Medicinal Crop Science
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• v.10 no.5
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• pp.399-402
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• 2002

Angiotensin converting enzyme(ACE) belongs to the class of zinc protease and plays an important role in the regulation of blood pressure. In this experiment, we investigated the inhibitory activities of medicinal plant extracts on ACE. Fifty medicinal plants were selected and the extracts were prepared by refluxing with 70% methanol. Among the extracts, eleven medicinal plant extracts such as Sedum sarmentosum Bunge, Petasites japonicus(s.et z.) Max, Rubus coreanus, Morus bombycis Koidz, Acorus calamus var. angustatus, Glycyrhiza glabra, Equisetum hyemale, Portulaca oleracea L., Prunella vulgaris var. lilacina Nakai, Sorbus commixta Hedl, Allium thunbergii showed more than 50% inhibitory activities, and Paeonia suffruticosa Andr., lnula helenium, Acanthopanax senticosus Harms, Dendrobium moniliforme, Juglans mandshurica, Zizyphus jujuba, Leonurus artemisia, Aster scaber Thunb, Vitex rotundifolia, Platycodon grandiflorum, Prunus persica, Ligularia fischeri showed $40{\sim}49%$ inhibitory activities. Therefore these extracts which contain high ACE inhibitory activities may be useful as antihypertension agents and to the treatment of hypertension.

• Journal of Life Science
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• v.10 no.2
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• pp.140-149
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• 2000

In order to utilize marine processing waste which would normally be discarded, cod liver protein was hydrolysed by ${\alpha}$-chymotrysin, and the hydrolysate was investigated for the new angiotensin I converting enzyme (ACE) inhibitor. Thy hydrolysate was separated into three major types, with molecular weight cut-off (MWCO) values less than 10 kDa, 5 kDa and 1 kDa of ultrafiltration membranes, respectively. ACE inhibitory peptides were isolated from the fractions passed through MWCO 1 kDa membrane, and purified by using ion-exchange chromatography on a SP-Sephadex C-25 column, gel filtration on a Sephadex G-15 column, and HPLC on an ODS column. The purity was identified with capillary electrophoresis. The amino acid sequences of two peptides were Met-Ile-Pro-Pro-Tyr-Tyr (IC50=10.9 ${\mu}$M) and Gly-Leu-Arg-Asn-Gly-Ile (IC50=35.0 ${\mu}$M)