• 한국식품저장유통학회:학술대회논문집
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• 한국식품저장유통학회 2003년도 제23차 추계총회 및 국제학술심포지움
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• pp.135.2-135
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• 2003

Angiotensin converting enzyme (ACE) converts angiotensin I into angiotensin II by cleaving C-terminal dipeptide of angiotensin I and inactivates bradykinin. ACE inhibitors have been screened from various food sources since the inhibitors decrease blood pressure. Therefore, in this study, an ACE inhibitor was isolated and purified from squid ink using membrane filtration, gel permeation chromatography, normal phase HPLC, and fast protein liquid chromatography. The purified inhibitor was identified to be a molecular mass of 294 by mass spectrometry, and to have IC$\sub$50/ value of 4.9 $\mu\textrm{g}$/mL.

• Asian-Australasian Journal of Animal Sciences
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• 제16권9호
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• pp.1369-1373
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• 2003

ACE (Angiotensin-I converting enzyme) inhibitory peptides derived from foods are thought to suppress high blood pressure by inhibiting ACE. We tried to make efficient production of the ACE inhibitory hydrolysate from egg albumen. A hydrolysate digested by neutrase presented the highest ACE inhibitory activity ($IC_50\;value=256.35{\mu}g/ml$) and the proper proteolysis was occurred by 1.0% enzyme addition and 4 h incubation at $47^{\circ}C$. Antihypertensive effect of neutrase hydrolysate was investigated in spontaneously hypertensive rats (SHR, n=5). Systolic blood pressure (SBP) was decrease by 6.88% (-14.14 mmHg, p<0.05) at 3 h after oral administration of 300 mg/kg body weight, and by 13.33% (-27.72 mmHg, p<0.05) by emulsified hydrolysate. These results showed that it is very effective to utilize egg albumen as a protein source for the production of ACE inhibitory peptides. However, further studies are required to investigate the methods to increase recovery yield and the isolation of active peptide is necessary for determining its sequence responsible for ACE inhibitory activity.

• Asian-Australasian Journal of Animal Sciences
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• 제16권3호
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• pp.417-424
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• 2003

Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, $\alpha$-chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and $\alpha$-chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by $\alpha$-chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.

• Preventive Nutrition and Food Science
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• 제20권3호
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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.

• 한국축산식품학회지
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• 제22권1호
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• pp.87-93
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• 2002

최근 고혈압을 예방하기 위한ACE 저해 펩타이드에 대한 연구는 주로 여러 가지 식품 단백질의 효소 가수분해물로부터 얻어진 펩타이드를 중심으로 이루어지고 있다. 본 연구에서는 케이신을 여러 가지 상업용 단백질분해 효소를 사용하여 ACE저해 효과가 높은 가수분해물 제조시 가수분해 조건이 ACE저해효과에 미치는 영향을 알아보자 하였으며 적정 가수분해 조건을 설정하고자 하였다. ACE 저해효과를 가지는 케이신 가수분해 물을 제조하기 위한 효소 종류, 첨가량 및 가수분해시간은 효소는 Aspergillus oryzae 유래의 promod 192를 사용하고, 효소의 첨가량은 케이신에 대하여 1%, 반응시간은 47$^{\circ}C$에서 12시간으로 하는 것이 적당하였다. 이 때 케이신 가수분해물의 $IC_{50}$/값은 248.71ug/m1(통상법), 265.84ug/ml(전처리법)로서 ACE 저해효과가 높았다.

• 한국식품과학회지
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• 제29권6호
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• pp.1269-1274
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• 1997

국내에서 재배된 Aloe vera에서 생리활성 물질인 acetylmannan을 분리 하고 그 제반의 특성을 규명하고 ACE저해효과 및 동력학적분석을 행한 결과 다음과 같은 결론을 얻었다. 알로에 베라 3.5 Kg으로 부터 에탄올에 불용성 다당체를 수득, 백색의 분말형태인 0.9 g의 acetylmannan을 얻었다. 분리한 acetylmannan은 탄수화물 67%를 함유하고 있으며 만노오즈는 60% 소량의 글루코오즈와 갈락토오즈로 이루어져 있고 아세틸기는 23%를 함유하고 있으며 acetyl group은 IR 스펙트럼에서 $1746\;cm^{-1}$, $1244\;cm^{-1}$ peak으로서 확인하였다. 과요오드 산화법에서 과요오드 음이온 소비량이 포름산 생성량에 비해 많고, 1, 4 글리코사이드 결합으로 이루어져 있음을 확인하였다. 또한 ACE에 대한 $IC_{-50}$ 값은 0.58 mM 이였으며, competitive 저해형식을 나타내었고. Ki 값은 0.068 mM 이였다.

• 자연과학논문집
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• 제16권1호
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• pp.1-13
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• 2005

안지오텐신(ACE) 저해제는 항고혈 효과를 갖고 있으므로 오랫동안 고혈압의 예방이나 치료에 이용되어 왔다. 본 연구는 재조합 대장균으로부터 새로운 ACE 저해제를 생산하고 정제하며 나아가 이들이 구조-기능 관P를 규명하기 위해 수행되었다. Saccharomyces cerevisiae의 ACE 저해 펩타이드 유전자를 함유하고 있는 재조합 pGEX-4T-3을 대장균 BL21(DE3)로 형질전환 시켰다. 재조합 pGEX-4T-3을 갖고 있는 대장균 BL21(DE3)로부터 생산된 Glutathione-s 전이효소(GST) 융합 단백질을 얻어서 그중 ACE저해 펩타이드를 Sephadex G-25 컬럼 크로마토그래피로 정제하였다. 정제된 ACE 저해 펩타이드는 타이로신-아스파틱엑시드-그리신-글리신-발린-페닐알라린-아르기닌-발린-타이로신-트레오닌의 서열을 가진 새로운 decapeptide이었고 ACE에 대하여 경쟁적으로 저해하였다.

• 한국미생물·생명공학회지
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• 제31권1호
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• pp.51-56
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• 2003

안정성이 확보된 식품에서 ACE저해 활성 물질을 검색하는 연구의 일환으로, 옥수수 글루텐을 Flavourzyme, Pescalase, 그리고 Thermolysine/Pescalase 등으로 가수분해하여 얻은 가수 분해물로부터 ACE 활성 저해 펩타이드를 다음과 같은 과정으로 분리, 정제하였다. 10% 에탄올로 평형화된 ODS chromatography를 이용 단백질 분획들을 얻고, Bio-Gel P-2 column과 reverse phase HPLC를 통해 5개의 ACE 저해 펩타이드를 분리, 정제하였다. 그 아미노산 서열은 LPF($IC_{50}$ = 40 $\mu$M), GPP($IC_{50}$ = 17.6 $\mu$M), PNPY($IC_{50}$ = 30.7 $\mu$M), SPPPFYL($IC_{50}$/ = 63 $\mu$M), and SQPP($IC_{50}$ = 17.2 $\mu$M)로 밝혀졌다. 이 펩타이드들은 경구투석 시 가수분해 효소에 대응하여 체내에서 안정성이 뛰어나고, 소장에서도 쉽게 흡수될 것으로 사료되어 상시 섭취하는 식품이나 음료에 첨가하여 이용한다면 그 유용성이 기대된다.

• 사상체질의학회지
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• 제14권1호
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• pp.132-139
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• 2002

The correlation between angiotensin converting enzyme (ACE) polymorphisms and cerebral infarction (CI) has been controversial. Such controversy may be due to different classifications of cerebrovascular diseases and ethnic differences. I studied the correlation between ACE genotypes and CI patients by case-control study in the Korean population. I also classified CI patients and control group into four types according to Sasang constitutional medicine. Furthermore I investigated the correlation among ACE genotypes, CI and Sasang constitutions. The frequencies of D allele were 0.32 in subjects with CI and 0.40 in the control group without CI (X2=0.128, p=0.720). In patients with CI, the frequency of Taeumins, one of four Sasang constitutional types, was significantly higher than that in controls (X2=15.425, p<0.00l). I did not find any correlation between ACE polymorphism and CI in Koreans. However, there were significant differences in allele frequencies between Koreans and Europeans, while similarities were shown to those of Japanese and Chinese populations.

• 대한의생명과학회지
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• 제18권4호
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• pp.406-412
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• 2012

The polymorphism (insertion, I or deletion, D) of angiotensin converting enzyme (ACE) gene is designated as the presence of a 287 bp Alu repeat. The D/D homozygote carrier is associated with high ACE activity, and this high activity has been implicated with hypertension, coronary artery disease, or diabetic nephropathy. We studied the clinical candidate marker in ACE gene polymorphism using chemical and hematological analysis. The subjects are divided into normotensive and hypertensive groups and ACE genotype in the group was confirmed by PCR method. Chemical analysis was preceded with Hitachi7060, and hematological analysis was performed using Mythic 22. In 116 targeted people, 17 (38.64%) of 44 I/I genotype group are hypertension, 15 (34.09%) in 44 with D/I, but, D/D type in the 28 cases is 15 patients (53.57%) in hypertension. In hypertension group, biochemical analysis (triglyceride, and alkaline phosphatase) and hematological analysis (white blood cell, platelet) are showed high value in D/D genotype of ACE gene. The relationship between hypertension and ACE genotype is the same results as previously reported and we thought that the high laboratory value of white blood cell, platelet, triglycerides, and alkaline phosphatase are also indicator of hypertension in D/D type of ACE.