• 한국식품과학회지
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• 제25권5호
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• pp.456-460
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• 1993

전통 기호음료 성분에 의하여 나타나는 기능특성을 조사하기 위한 연구의 일환으로 결명자,들깨, 대추, 모과, 오미자, 오갈피 및 생강 추출물을 ion-exchange chromatography, 유기용매에 의한 분획, silica gel column chromatography, thin layer chromatography에 의하여 여러 가지 획분으로 분획하여 Angiotensin I 전환효소(ACE) 저해작용을 조사한 결과는 다음과 같다. 기호음료 원료에서 추출한 수용성 획분의 ACE 저해작용은 생강>오갈피>오미자>들깨>결명자>모과>대추의 순으로 나타났다. 일반 가정에서 널리 이용되고 있는 결명자에서 분리한 compound C 는 ACE 저해제로 알려져 있는 bradykinin에 비하여 ACE 저해작용이 비교적 낮았다.

• Asian-Australasian Journal of Animal Sciences
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• 제18권5호
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• pp.741-746
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• 2005

To investigate the basic information and the possibility of ACE-inhibitory peptides for antihypertension materials, goat's caisin (CN) was hydrolyzed by various proteolytic enzymes and ACE-inhibitory peptides were separated and purified. ACE-inhibition ratios of enzymatic hydrolysates of goat's CN and various characteristics of ACE-inhibitory peptides were determined. ACE-inhibition ratios of goat's CN hydrolysates were shown the highest with 87.84% by pepsin for 48 h. By Sephadex G-25 gel chromatograms, Fraction 3 from goat's CN hydrolysates by pepsin for 48 h was confirmed the highest ACE-inhibition activity. Fraction 3 g and Fraction 3 gh from peptic hydrolysates by RP-HPLC to first and second purification were the highest in ACE-inhibition activity, respectively. The most abundant amino acid was leucine (18.83%) in Fraction 3 gh of ACE-inhibitory peptides after second purification. Amino acid sequence analysis of Fraction 3 gh of ACE-inhibitory peptides was shown that the Ala-Tyr-Phe-Tyr, Pro-Tyr-Tyr and Tyr-Leu. IC$_{50}$ calibrated in peptic hydrolysates at 48 h, Fraction 3, Fraction 3 g and Fraction 3 gh from goat's CN hydrolysates by pepsin for 48 h were 29.89, 3.07, 1.85 and 0.87 g/ml, respectively. Based on the results of this experiment, goat's CN hydrolysates by pepsin were shown to have ACE-inhibitory activity.

• 한국식품과학회지
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• 제30권6호
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• pp.1476-1479
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• 1998

키토산 올리고당이 ACE 저해활성과 SHR의 혈압에 미치는 영향을 검토하였다. 키토산 올리고당은 모두 ACE 저해활성을 나타내었다. ACE 저해활성$(IC_{50})$은 3량체가 $0.9\;{\mu}mole$로 가장 우수하였고 2량체의 경우에는 $2.4\;{\mu}mole$, 그 외의 올리고당은 모두 $>100\;{\mu}mole$였다. 강력한 ACE 저해제인 Captopril(2-D-mercaptopropanoyl-L-proline)의 인체 투여량을 기준으로 3량체 키토산 올리고당 2.14 mg/kg을 SHR에 강제 경구투여한 바, 4시간 경에 8주령 및 21주령 SHR모두 최저혈압을 보였고 이 때의 혈압 강하는 8주령 SHR $27{\pm}4.8\;mmHg$, 21주령 SHR $36{\pm}4.3\;mmHg$로 나타났다. 따라서 3량체 키토산 올리고당은 2량체 키토산 올리고당과 함께 향후 고혈압 치료제로서 응용가능함이 시사되었다.

• 한국축산식품학회:학술대회논문집
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• 한국축산식품학회 2005년도 제36차 추계 학술발표대회
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• pp.329-333
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• 2005

ACE inhibition activity of peptides was measured after 2 months of storage at $4^{\circ}C$ under condition of pH 6.0, 6.5, 7.0, 7.5, 8.0. and the ACE inhibitory activity were changed only slightly. After 2 months of chilled storage ($4^{\circ}C$), no dramatic change and significance was found. This indicates that acidic, neutral, weak alkali conditions did not affect ACE inhibitory activity of those peptides. Among peptide 1134, 1152, and 1155, peptides from thermolysin + protease A hydrolysates, inhibition activity of peptide 1134 and 1152 was decreased significantly at $60^{\circ}C$, however, they showed stable inhibition activity from $70^{\circ}C$ to $100^{\circ}C$ (P<0.001). Also, chromatogram of peptide 1134, 1152, and 1155 was shown that retention time of peptide of $60^{\circ}C$ was not correspond to the retention time of the rest of peptides. This indicated that temperature may change the inhibitory activity and profile of peptides.

• 한국식품영양과학회지
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• 제27권4호
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• pp.751-755
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• 1998

Functional properties of yam mucilage were investigated by physicochemical analysis. Yam mucilage was extracted from the root of yam and then separated into two fractions by its selective aggregation with isopropanol concentration. Each mucilge fraction showed the excellent binding properties with heavy metal ions Co, Cr and Cu. Cr showed the higher affinity with mucilage than Co and Cu at pH 6.3. In ACE inhibition, IC50 values of mucilage fraction 1 and 2 showed 8.99$\mu\textrm{g}$/${mu}ell$ and 7.1$\mu\textrm{g}$/${mu}ell$, respectively.

• 한국축산식품학회지
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• 제25권2호
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• pp.238-243
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• 2005

산양유 $\beta-casein$의 효소에 의한 가수분해 특성과 가수분해물의 ACE 저해 효과를 측정하고자 산양유의 $\beta-casein$을 양이온 교환 컬럼인 Mono S HR 5/5를 이용하여 분리하였으며 분리된 $\beta-casein$을 동물성 분해효소인 trypsin으로 처리하여 가수분해 특성을 확인하였고 가수분해물의 ACE 저해활성을 측정하였다. Mono S HR 5/5 양이온 교환 컬럼을 이용한 산양유 산 케이신으로 부터 순수한 $\beta-casein$의 분리는 SDS-PAGE를 이용하여 확인한 결과 순수한 $\beta-casein$의 분리가 이루어졌음을 확인할 수 있었다. $\beta-casein$을 $37^{\circ}C4$에서 trypsin으로 처리하여 전기영동으로 확인한 결과 가수분해 직후부터 $\beta-casein$ 위치의 band가 희미해지기 시작하고 저분자량의 band가 나타나기 시작하였으나 120분이 지난 후에는 모든 band가 가수분해되어 사라졌고 산양유에서 분리된 $\beta-casein$을 trypsin으로 처리하여 120분 경과 후 그 가수분해물을 이용하여 ACE 저해효과를 측정한 결과 가수분해하지 않은 $\beta-casein$은 $1.80\pm1.21\%$의 ACE 저해활성을 보였으나 trypsin으로 가수분해하여 ACE 저해 활성을 측정하였을 때 $25.36\pm0.79\%$의 저해 활성을 나타내었으며, trypsin에 의한 $\beta-casein$가수분해물의 $IC_{50}$을 측정한 결과 $308.7\pm2.77({\mu}g/mL)$로 나타났다.

• BMB Reports
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• 제31권5호
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• pp.459-467
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• 1998

A new set of functional group interaction energy descriptors relevant to the ACE (Angiotensin-Converting Enzyme) inhibitory peptide, QSAR (Quantitative Structure Activity Relationships), is presented. The functional group interaction energies approximate the charged interactions and distances between functional groups in molecules. The effective energies of the computationally derived geometries are useful parameters for deriving 3D-QSAR models, especially in the absence of experimentally known active site conformation. ACE is a regulatory zinc protease in the renin-angiotensin system. Therapeutic inhibition of this enzyme has proven to be a very effective treatment for the management of hypertension. The non bond interaction energy values among functional groups of six-feature of ACE inhibitory peptides were used as descriptor terms and analyzed for multivariate correlation with ACE inhibition activity. The functional group interaction energy descriptors used in the regression analysis were obtained by a series of inhibitor structures derived from molecular mechanics and semi-empirical calculations. The descriptors calculated using electrostatic and steric fields from the precisely defined functional group were sufficient to explain the biological activity of inhibitor. Application of the descriptors to the inhibition of ACE indicates that the derived QSAR has good predicting ability and provides insight into the mechanism of enzyme inhibition. The method, functional group interaction energy analysis, is expected to be applicable to predict enzyme inhibitory activity of the rationally designed inhibitors.

• Applied Biological Chemistry
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• 제37권6호
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• pp.441-446
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• 1994

된장의 새로운 기능성을 검색하기 위해 된장의 ACE 활성 저해효과를 측정하였다. 7개의 시중제품중 ACE 활성 저해효과가 가장 높은 된장의 열수추출물을 용매별 분획시 acetone$(50{\sim}80%)$ 분획이 acetonitrile$(50{\sim}80%)$ 분획에 비해 다소 낮은 57% 단백질 회수율을 보였으나, ACE 활성 저해효과는 92.8%로 가장 높은 활성 저해효과를 보였다. 아세톤 분획을 Sephadex G-25, Sephadex LH-20, ODS column chromatography와 HPLC를 이용하여 정제한 결과 수율은 1%, $IC_{50}$ 값은 0.6 mg/ml로 나타났다. 된장으로부터 정제한 저해물질은 경쟁적 저해기작을 나타냈으며, 아미노산 분석결과 Ala, Phe, Leu, Glu, Gly, Ser, Asp 아미노산으로 구성되어 있었다.

• 한국식품과학회지
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• 제38권5호
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• pp.691-698
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• 2006

본 연구는 혈액순환 개선 효능을 알아보기 위해 민간에서 빈번하게 사용하는 허브류인 마조람, 라벤더, 딜, 로즈마리, 히솝, 장미, 레몬밤, 파인애플 세이지 및 에키네시아 등 총 9종 을 실험 시료로 선정하였다. 이들을 부위별 및 용매별로 추출하여 angiotensin I converting enzyme(ACE) 저해 활성, hydroxy-methylglutalyl coenzyme A reductase 저해활성 및 혈전용해활성을 측정하였다. 추출 수율은 장미꽃이 가장 높았으며 열수 추출의 경우 43.3%였고 70% 에탄올 추출의 경우 45%였다. ACE 저해활성은 열수 추출의 경우 장미꽃이 133.8% 로 가장 높았고 70% 에탄올 추출의 경우에는 파인애플 세이지 잎이 91.2%로 가장 높았다. HMG-CoA reductase 저해활성의 경우에는 장미꽃이 열수 추출물 48.9%, 70% 에탄올 추출물 80.5%로 모두 높았다. 혈전용해활성도 장미꽃에서 열수 추출이나 에탄올 추출물 모두 가장 높은 활성을 보였다. 이상의 결과로 볼 때 장미꽃 추출물의 혈액순환 개선 효과가 뛰어난 것으로 나타나 기능성 식품으로의 개발 가능성이 기대된다.

• Food Science and Biotechnology
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• 제18권2호
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• pp.541-545
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• 2009

Water and ethanol extracts were prepared from the haesongi mushroom (Hypsizigus marmoreus) to measure functional components. The ability of the extracts to inhibit angiotensin-converting enzyme (ACE) and their hypoglycemic effects were also determined; the latter was measured by $\alpha$-amylase and glucosidase inhibition. Extraction yield, protein content, total phenol, and $\beta$-glucan in the water extracts were 55.86, 17.71, 1.89, and 21.93%, respectively. The respective values for the ethanol extracts were lower than those for water extracts. Both water and ethanol extracts showed dosedependent ACE inhibition, the effect of the former being greater. The water extract inhibited ACE activity by 95.34% at 40 mg/mL. The $IC_{50}$ values of the water extracts were 63.32 and 0.41 mg/mL for $\alpha$-amylase and glucosidase, respectively. Thus, the water extracts had a greater hypoglycemic effect than the ethanol extracts. From these results, water is a better solvent than ethanol to extract from the haesongi mushroom functional components that show ACE inhibition and have hypoglycemic effects.