• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.2
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• pp.226-233
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• 1993

Enzymatic hydrolysates of food proteins (defatted soybean cake, egg albumin and casein) were tested for inhibitory activity against angiotensin-I converting enzyme (ACE). Food proteins were hydrolysed with complex enzyme, bromelain, alcalase, $\alpha$-chymotrypsin, trypsin, papain and pepsin by heating method. The hydrolysates obtained from the treatment of complex enzyme and bromelain showed the higher ACE inhibitory activity. ACE inhibitory activity of hydrolysates exhibited a tendency to be increased until 8hrs and increased with increment of concentration. The activity was also stable by heat treatment at 10$0^{\circ}C$ for 20min. Molecular weight of active fraction was about 1, 400 and defatted soybean cake hydrolysate below 1, 400 in case of defatted soybean cake hydrolysate treated with alcalase. Amino acid of the active fractions was abundant in Asp, Glu, Lys, lle, Leu, Ala and Val.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2001.10a
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• pp.171-172
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• 2001

체내에 널리 분포되어 있는 angiotensin 전환효소(angiotensin converting enzyme, ACE ; peptidyldipeptide hydrolase, EC 3.4.15.1)는 angiotensinogen이 renin의 특이적 분해를 받아서 생성된 불활성형인 angiotensin I의 말단 dipeptide(His-Leu)를 절단하여 octapeptide인 활성형의 angiotensin II로 전환시키며, 이렇게 생성된 angiotensin II는 직접적으로 혈압상승 작용을 하거나 adrenal로부터 sediumretaining steroid hormone인 aldosterone의 유리를 촉진시켜 체내 나트륨을 저류시킨다. (중략)

• 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.20 no.5
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• pp.768-774
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• 2010

In this study, we investigated the antioxidant activities, alcohol metabolizing activities, nitrite scavenging ability, angiotensin converting enzyme (ACE), and elastase inhibitory effects of hot water extract from Makgeoly (HWM). Antioxidant activities were measured by using 2,2.diphenyl.1.picryl.hydrazyl (DPPH) free radical scavenging activity and SOD (superoxide dismutase).like activity. The DPPH radical scavenging activity and SOD.like activity of HWM were remarkably increased in a dose.dependent manner and were 48.0% and 98.7% at 10 mg/ml, respectively. To determine the influence of HWM on alcohol metabolizing activity, the generating activities of reduced.nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured. The facilitating rates of ADH and ALDH activity by HWM were remarkably increased in a dose.dependent manner and were 70.2% and 64.1% at 10 mg/ml, respectively. The inhibitory activity against angiotensin converting enzyme (ACE) of HWM was increased in a dose.dependent manner and was 74.2% at 10 mg/ml. The nitrite scavenging ability of HWM showed the most remarkable effect at pH 1.2 and 2 mg/ml. These results indicated that HWM may have valuable biological properties owing to their antioxidant activities, ADH and ALDH activity, nitrite scavenging ability, and ACE inhibitory activity.

• Tuberculosis and Respiratory Diseases
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• v.52 no.5
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• pp.506-518
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• 2002

Background : There have been several studies showing that angiotensin II and the angiotensin converting enzyme (ACE) contribute to the activation of fibroblast including the pulmonary fibrosis, and apoptosis of the alveolar epithelium in idiopathic intersititial pneumonia. This study was performed to identify the relationship between the serum angiotensin II, ACE and the pulmonary function test (PFT), the dyspnea score, and the cell fraction of the bronchoalveolar lavage fluid(BALF). Materials and Methods : Twenty three patients with idiopathic interstitial pneumonia from March, 1999 to October, 2001 at Gachon medical school were enrolled in this study. They were divided into IPF(UIP) (16) and NSIP (7) groups. Twelve of the idiopathic interstitial pneumonia patients (UIP : 5, NSIP : 7) were diagnosed by an open lung biopsy, 11 of IPF patients were diagnosed by the American Thoracic Society (ATS) diagnostic criteria. The PFT values, dyspnea score, serum ACE and angiotensin II were measured, and a bronchoscopy was performed to obtain the BALF. Results : Of all the patients, 7 were in the normal range and 14 showed an increase in the serum level of angiotensin II. In terms of the serum ACE level, 14 patients had an increased level. The DLCO% of the angiotensin II in increased group was significantly lower than the not-increased group (p=0.021). Other factors did not correlate with the serum ACE or the angiotensin II increased group and not-increased group. Conclusion : These results suggest that an increased angiotensin II serum level may be associated with increase in the of alveolar capillary block in the progression of pulmonary fibrosis in idiopathic interstitial pneumonia.

• Korean Journal of Food Science and Technology
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• v.33 no.1
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• pp.84-88
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• 2001

About 100 bacterial strains producing proteolytic enzymes were isolated from Korean traditional soy paste Doenjang. Among them, strain SYG3 producing the highest level of angiotensin converting enzyme (ACE) inhibitor into the culture medium was selected and identified as Bacillus pumilus according to the Bergey's mannual of systematic bacteriology. Soybean powder as a nitrogen source and glucose as a carbon source supported high level of ACE inhibitor production. The presence of 3% NaCl also enhanced the production of ACE inhibitor in the medium. The optimum initial pH of the medium and culture temperature for the production of ACE inhibitor were 7.0 and $32^{\circ}C$, respectively. The maximal level of ACE inhibitory effect was obtained after 36 hours of cultivation under the optimized conditions, which was about 98% of inhibition ratio.

• Journal of Veterinary Science
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• v.24 no.2
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• pp.26.1-26.11
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• 2023

Background: Angiotensin-converting enzyme inhibitor (ACEi) inhibits the catalysis of angiotensin I to angiotensin II and the degradation of substance P (SP) and bradykinin (BK). While the possible relationship between ACEi and SP in nociceptive mice was recently suggested, the effect of ACEi on signal transduction in astrocytes remains unclear. Objectives: This study examined whether ACE inhibition with captopril or enalapril modulates the levels of SP and BK in primary cultured astrocytes and whether this change modulates PKC isoforms (PKCα, PKCβI, and PKCε) expression in cultured astrocytes. Methods: Immunocytochemistry and Western blot analysis were performed to examine the changes in the levels of SP and BK and the expression of the PKC isoforms in primary cultured astrocytes, respectively. Results: The treatment of captopril or enalapril increased the immunoreactivity of SP and BK significantly in glial fibrillary acidic protein-positive cultured astrocytes. These increases were suppressed by a pretreatment with an angiotensin-converting enzyme. In addition, treatment with captopril increased the expression of the PKCβI isoform in cultured astrocytes, while there were no changes in the expression of the PKCα and PKCε isoforms after the captopril treatment. The captopril-induced increased expression of the PKCβI isoform was inhibited by a pretreatment with the neurokinin-1 receptor antagonist, L-733,060, the BK B1 receptor antagonist, R 715, or the BK B₂ receptor antagonist, HOE 140. Conclusions: These results suggest that ACE inhibition with captopril or enalapril increases the levels of SP and BK in cultured astrocytes and that the activation of SP and BK receptors mediates the captopril-induced increase in the expression of the PKCβI isoform.

• Food Science and Biotechnology
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• v.16 no.4
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• pp.565-571
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• 2007

This study was carried out to investigate an optimum condition for the high angiotensin-l converting enzyme (ACE) inhibitory activity and the yield on enzyme concentration, casein concentration, and hydrolysis time. The optimum condition was performed by response surface methodology for acquirement of casein hydrolysate of milk which shows high ACE inhibitory activity, Among 8 tested enzymes, Protamex showed the highest activation degree with 77.03 unit/g from casein. Their hydrolysis degrees of flovourzyme 500MG, protamex, mixture from 1% casein were 85.5, 88.5, and 93.5%, respectively. The ranges of enzyme concentration (0.25-1.25%), casein concentration (2.5-12.5%), and hydrolysis time (20-100 min) as 3 independent variables through preliminary experiments of the yield of casein hydrolysate and ACE inhibitory activity, and it shows optimum response surface at a saddle point. It shows enzyme concentration (0.64%), casein concentration (8.38%), and hydrolysis time (55.81 min) in the yield aspect and showed the highest activity at enzyme concentration (0.86%), casein concentration (5.97%), and hydrolysis time (63.86 min) in ACE inhibitory aspect. The $R^2$ value of a fitted optimum formula on the hydrolysis yield was 0.9751 as the significant level of 1%. The $R^2$ value of a fitted optimum formula on ACE inhibitory activity is 0.8398, and the significance is recognized in the range of 5%.

• 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.

• Clinical and Experimental Pediatrics
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• v.64 no.5
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• pp.225-226
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• 2021